Catalase and its mysteries
Catalase is one of the firsts in every realm of biological sciences. At the same time it also has a number of unusual features. It has one of the highest turnover numbers of all enzymes. It is essential for neutralizing the noxious hydrogen peroxide both in the nature and the various industries such...
Saved in:
| Published in | Progress in biophysics and molecular biology Vol. 140; pp. 5 - 12 |
|---|---|
| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
England
Elsevier Ltd
01.12.2018
|
| Subjects | |
| Online Access | Get full text |
| ISSN | 0079-6107 1873-1732 1873-1732 |
| DOI | 10.1016/j.pbiomolbio.2018.03.001 |
Cover
Loading…
| Abstract | Catalase is one of the firsts in every realm of biological sciences. At the same time it also has a number of unusual features. It has one of the highest turnover numbers of all enzymes. It is essential for neutralizing the noxious hydrogen peroxide both in the nature and the various industries such as dairy, textile and pharmaceutics. It also has the merit of being one of the first protein crystals to be isolated. Ironically its three-dimensional structure was discerned some forty years later. However through the times this senile enzyme has continued to intrigue the scientists by surprising facts and phenomena, such as peculiar interweaving of subunits and remarkable thermal stability. It is also known for suicide inactivation by its own substrate. Catalase is known to be implicated in various medical scenarios and its levels have served as a marker in that capacity. It has even been incorporated into several pharmaceuticals. This review strives to clarify these perspectives. It also draws attention to the biophysical contributions offered by thermodynamics and kinetics in these discoveries. The ultimate aim of this review, however, is to state that the venerable catalase will continue to bewilder us with its mysteries well into the twenty-first century. |
|---|---|
| AbstractList | Catalase is one of the firsts in every realm of biological sciences. At the same time it also has a number of unusual features. It has one of the highest turnover numbers of all enzymes. It is essential for neutralizing the noxious hydrogen peroxide both in the nature and the various industries such as dairy, textile and pharmaceutics. It also has the merit of being one of the first protein crystals to be isolated. Ironically its three-dimensional structure was discerned some forty years later. However through the times this senile enzyme has continued to intrigue the scientists by surprising facts and phenomena, such as peculiar interweaving of subunits and remarkable thermal stability. It is also known for suicide inactivation by its own substrate. Catalase is known to be implicated in various medical scenarios and its levels have served as a marker in that capacity. It has even been incorporated into several pharmaceuticals. This review strives to clarify these perspectives. It also draws attention to the biophysical contributions offered by thermodynamics and kinetics in these discoveries. The ultimate aim of this review, however, is to state that the venerable catalase will continue to bewilder us with its mysteries well into the twenty-first century. Catalase is one of the firsts in every realm of biological sciences. At the same time it also has a number of unusual features. It has one of the highest turnover numbers of all enzymes. It is essential for neutralizing the noxious hydrogen peroxide both in the nature and the various industries such as dairy, textile and pharmaceutics. It also has the merit of being one of the first protein crystals to be isolated. Ironically its three-dimensional structure was discerned some forty years later. However through the times this senile enzyme has continued to intrigue the scientists by surprising facts and phenomena, such as peculiar interweaving of subunits and remarkable thermal stability. It is also known for suicide inactivation by its own substrate. Catalase is known to be implicated in various medical scenarios and its levels have served as a marker in that capacity. It has even been incorporated into several pharmaceuticals. This review strives to clarify these perspectives. It also draws attention to the biophysical contributions offered by thermodynamics and kinetics in these discoveries. The ultimate aim of this review, however, is to state that the venerable catalase will continue to bewilder us with its mysteries well into the twenty-first century.Catalase is one of the firsts in every realm of biological sciences. At the same time it also has a number of unusual features. It has one of the highest turnover numbers of all enzymes. It is essential for neutralizing the noxious hydrogen peroxide both in the nature and the various industries such as dairy, textile and pharmaceutics. It also has the merit of being one of the first protein crystals to be isolated. Ironically its three-dimensional structure was discerned some forty years later. However through the times this senile enzyme has continued to intrigue the scientists by surprising facts and phenomena, such as peculiar interweaving of subunits and remarkable thermal stability. It is also known for suicide inactivation by its own substrate. Catalase is known to be implicated in various medical scenarios and its levels have served as a marker in that capacity. It has even been incorporated into several pharmaceuticals. This review strives to clarify these perspectives. It also draws attention to the biophysical contributions offered by thermodynamics and kinetics in these discoveries. The ultimate aim of this review, however, is to state that the venerable catalase will continue to bewilder us with its mysteries well into the twenty-first century. |
| Author | Moosavi-Movahedi, Ali Akbar Sepasi Tehrani, Hessam |
| Author_xml | – sequence: 1 givenname: Hessam surname: Sepasi Tehrani fullname: Sepasi Tehrani, Hessam email: sepasi@srbiau.ac.ir organization: Department of Biology, Islamic Azad University, Science and Research Branch, Tehran, Iran – sequence: 2 givenname: Ali Akbar surname: Moosavi-Movahedi fullname: Moosavi-Movahedi, Ali Akbar organization: Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/29530789$$D View this record in MEDLINE/PubMed |
| BookMark | eNqNkMtKxDAUhoMozkVfwIV06ab1pGmbdiPo4A0G3Og6nCankKGXMckI8_Z2mBkEN7o5Z_Nf-L8ZO-2HnhiLOCQceHG7Sta1HbqhHW-SAi8TEAkAP2FTXkoRcynSUzYFkFVccJATNvN-BQApl8U5m6RVLkCW1ZRdLTBgi54i7E1kg4-6rQ_kLPkLdtZg6-ny8Ofs4-nxffESL9-eXxf3y1gLmYVY502OWOelMRXHRtfIsWhkmnENOVJWpFmWGgllQxIg4yIHbooSdSMqBKPFnN3sc9du-NyQD6qzXlPbYk_Dxqtxn8h5VVTVKL0-SDd1R0atne3QbdVxzyi42wu0G7x31ChtAwY79MGhbRUHtQOoVuoH4K6gVCDUCHAMKH8FHDv-YX3YW2mE9WXJKa8t9ZqMdaSDMoP9O-QbqgaPlw |
| CitedBy_id | crossref_primary_10_1016_j_actbio_2023_03_030 crossref_primary_10_1111_1750_3841_15827 crossref_primary_10_31083_j_fbl2811313 crossref_primary_10_1016_j_aqrep_2022_101458 crossref_primary_10_1016_j_cbpb_2024_110983 crossref_primary_10_1021_jacs_0c00285 crossref_primary_10_3389_fphar_2023_1215020 crossref_primary_10_1007_s12010_020_03393_9 crossref_primary_10_1016_j_cryobiol_2024_104860 crossref_primary_10_3389_fphar_2024_1474678 crossref_primary_10_3390_ani14111549 crossref_primary_10_1016_j_crfs_2022_09_015 crossref_primary_10_1155_2020_5238650 crossref_primary_10_3390_oxygen4010007 crossref_primary_10_1007_s11356_022_19364_y crossref_primary_10_3390_antiox8060179 crossref_primary_10_3390_biom9100562 crossref_primary_10_3390_cancers12071706 crossref_primary_10_1016_j_ijbiomac_2023_128839 crossref_primary_10_1016_j_envres_2020_109923 crossref_primary_10_1007_s11626_018_0300_4 crossref_primary_10_1093_biomethods_bpae015 crossref_primary_10_3390_oxygen4010003 crossref_primary_10_1038_s41538_022_00146_2 crossref_primary_10_1016_j_ijbiomac_2022_11_266 crossref_primary_10_1111_jocd_15924 crossref_primary_10_3390_antiox9121292 crossref_primary_10_1016_j_fsi_2020_04_056 crossref_primary_10_1016_j_ijbiomac_2020_04_172 crossref_primary_10_1186_s12951_024_02850_5 crossref_primary_10_25289_ML_22_047 crossref_primary_10_1111_jfbc_13612 crossref_primary_10_1142_S2661318224300046 crossref_primary_10_1016_j_aquatox_2024_107157 crossref_primary_10_1016_j_optlastec_2024_111292 crossref_primary_10_1111_1749_4877_12602 crossref_primary_10_1002_fsn3_2684 crossref_primary_10_1016_j_ijbiomac_2023_124677 crossref_primary_10_1016_j_ctim_2019_03_016 crossref_primary_10_1007_s12668_024_01761_x crossref_primary_10_1186_s12906_024_04686_w crossref_primary_10_1016_j_ijbiomac_2019_06_139 crossref_primary_10_1016_j_neulet_2020_135484 crossref_primary_10_1021_acs_molpharmaceut_2c00215 crossref_primary_10_1093_genetics_iyab057 crossref_primary_10_1016_j_mcat_2023_113214 crossref_primary_10_1016_j_jelechem_2024_118093 crossref_primary_10_1016_j_jsps_2022_09_011 crossref_primary_10_1016_j_pbb_2022_173468 crossref_primary_10_3390_ijms25021283 crossref_primary_10_1016_j_fct_2024_114738 crossref_primary_10_1016_j_cclet_2022_03_054 crossref_primary_10_3390_antiox13020144 crossref_primary_10_3390_ph13110379 crossref_primary_10_1002_anie_202418725 crossref_primary_10_2147_JIR_S369176 crossref_primary_10_3389_fnut_2023_1275199 crossref_primary_10_1016_j_apsusc_2022_155816 crossref_primary_10_31883_pjfns_185366 crossref_primary_10_1080_15287394_2021_1975589 crossref_primary_10_1016_j_freeradbiomed_2018_07_021 crossref_primary_10_3390_plants10061089 crossref_primary_10_1155_2020_7340312 crossref_primary_10_1177_1352458519893925 crossref_primary_10_7717_peerj_15829 crossref_primary_10_1016_j_scitotenv_2023_167264 crossref_primary_10_1016_j_ijbiomac_2021_03_074 crossref_primary_10_1002_adhm_202401713 crossref_primary_10_1111_are_15287 crossref_primary_10_3390_antiox13040444 crossref_primary_10_1007_s00128_024_03930_w crossref_primary_10_1038_s41467_023_44026_z crossref_primary_10_1016_j_biopha_2023_114606 crossref_primary_10_1016_j_pbiomolbio_2019_08_008 crossref_primary_10_1016_j_ecoenv_2022_114146 crossref_primary_10_3390_ijms222312753 crossref_primary_10_2174_1574888X16666211206150934 crossref_primary_10_1590_2317_1545v43247033 crossref_primary_10_1007_s12088_020_00878_3 crossref_primary_10_3390_antiox10060985 crossref_primary_10_3390_chemosensors12090176 crossref_primary_10_3390_life13020331 crossref_primary_10_1155_2021_3155962 crossref_primary_10_3390_antiox10091442 crossref_primary_10_3390_antiox11010021 crossref_primary_10_1371_journal_pone_0282531 crossref_primary_10_1016_j_chemosphere_2023_138199 crossref_primary_10_1016_j_jece_2020_104517 crossref_primary_10_1002_ange_202418725 crossref_primary_10_1007_s11368_020_02741_w crossref_primary_10_1155_2018_9643721 crossref_primary_10_3390_ani13243830 crossref_primary_10_3390_ijms22136868 crossref_primary_10_3390_polym16131762 crossref_primary_10_3390_antiox11061131 crossref_primary_10_1051_e3sconf_202021006014 crossref_primary_10_1016_j_scitotenv_2023_165732 crossref_primary_10_1016_j_scitotenv_2022_158101 crossref_primary_10_1016_j_ijbiomac_2020_11_044 crossref_primary_10_1002_anbr_202400093 crossref_primary_10_1111_1462_2920_16305 crossref_primary_10_1016_j_pnpbp_2019_109708 crossref_primary_10_1039_d0mt00165a crossref_primary_10_1016_j_isci_2024_108977 crossref_primary_10_1016_j_procbio_2020_04_014 crossref_primary_10_3390_biology14010087 crossref_primary_10_5650_jos_ess21053 crossref_primary_10_1007_s00300_021_03001_4 crossref_primary_10_3390_jcm10071540 crossref_primary_10_3390_antiox13010018 crossref_primary_10_1016_j_aquatox_2023_106640 crossref_primary_10_1002_star_202200009 crossref_primary_10_3390_ani10020209 crossref_primary_10_1080_10643389_2021_1989235 crossref_primary_10_3390_antiox10071013 crossref_primary_10_3390_jpm11121281 crossref_primary_10_1016_j_aqrep_2023_101574 crossref_primary_10_3390_antiox9090864 crossref_primary_10_3390_cells7100156 crossref_primary_10_1016_j_saa_2023_122342 crossref_primary_10_1016_j_heliyon_2020_e04999 crossref_primary_10_3892_ijfn_2021_15 crossref_primary_10_1002_1873_3468_14906 crossref_primary_10_2217_nnm_2019_0166 crossref_primary_10_3390_en17123031 crossref_primary_10_1016_j_chemosphere_2022_133808 crossref_primary_10_1016_j_tiv_2020_104996 crossref_primary_10_1007_s11897_024_00645_1 crossref_primary_10_1002_aoc_7763 crossref_primary_10_1111_rda_14546 crossref_primary_10_1016_j_ijbiomac_2022_04_013 crossref_primary_10_1016_j_ijbiomac_2020_05_138 crossref_primary_10_1016_j_arabjc_2023_105393 crossref_primary_10_1016_j_jhazmat_2023_131496 crossref_primary_10_3390_antiox11122375 crossref_primary_10_3390_antiox13010038 crossref_primary_10_1016_j_scitotenv_2025_178868 crossref_primary_10_1038_s41598_020_62776_4 crossref_primary_10_1007_s00253_024_13395_w crossref_primary_10_1016_j_phymed_2024_156040 crossref_primary_10_1155_2022_8371440 crossref_primary_10_3390_md20030188 crossref_primary_10_3389_fcell_2021_720623 crossref_primary_10_1007_s40200_022_01179_w crossref_primary_10_1021_acs_chemrestox_2c00396 crossref_primary_10_3390_antiox10010089 crossref_primary_10_1172_jci_insight_140109 crossref_primary_10_3390_nano11030803 crossref_primary_10_1016_j_lwt_2021_110879 crossref_primary_10_3390_antiox10020276 crossref_primary_10_1016_j_ijbiomac_2019_07_197 crossref_primary_10_1007_s10499_024_01792_x crossref_primary_10_1007_s12011_022_03215_5 crossref_primary_10_1016_j_freeradbiomed_2020_08_013 crossref_primary_10_1016_j_cbpa_2024_111593 crossref_primary_10_1111_febs_15244 crossref_primary_10_3390_molecules24173058 crossref_primary_10_1002_lol2_10233 crossref_primary_10_1016_j_exppara_2024_108862 crossref_primary_10_1039_D2FO02910C crossref_primary_10_1039_D4EM00446A crossref_primary_10_1590_1807_1929_agriambi_v27n1p18_25 crossref_primary_10_3390_medicina58101491 crossref_primary_10_3390_antiox9060560 crossref_primary_10_1016_j_cbpa_2023_111503 crossref_primary_10_3390_nu15092029 crossref_primary_10_3389_fcell_2023_1290046 crossref_primary_10_1016_j_freeradbiomed_2021_11_016 crossref_primary_10_3390_horticulturae9030315 crossref_primary_10_1007_s13738_021_02321_w crossref_primary_10_1016_j_molstruc_2023_135310 crossref_primary_10_1021_acs_jpcb_2c05784 crossref_primary_10_1088_1755_1315_403_1_012113 crossref_primary_10_1016_j_freeradbiomed_2020_04_010 crossref_primary_10_3389_fncel_2022_963169 crossref_primary_10_3390_ijms25010070 crossref_primary_10_1007_s11033_018_4531_y crossref_primary_10_17221_133_2023_CJAS crossref_primary_10_2147_DDDT_S286104 crossref_primary_10_1016_j_scitotenv_2023_162634 crossref_primary_10_3389_fsufs_2024_1465445 crossref_primary_10_3390_antiox10020248 crossref_primary_10_3389_fvets_2024_1484388 crossref_primary_10_3390_ani13172789 crossref_primary_10_3390_app142210437 crossref_primary_10_3390_ijms21239149 crossref_primary_10_1615_JLongTermEffMedImplants_2023047580 crossref_primary_10_1016_j_fuel_2020_117795 crossref_primary_10_1007_s13738_021_02416_4 crossref_primary_10_1111_ijd_17718 crossref_primary_10_1016_j_jbiosc_2021_09_012 crossref_primary_10_1093_femsyr_foad052 crossref_primary_10_1016_j_foodchem_2025_144018 crossref_primary_10_1515_oncologie_2023_0472 crossref_primary_10_1002_cctc_202300491 crossref_primary_10_1080_10242422_2021_1932838 crossref_primary_10_1007_s11356_024_32926_6 crossref_primary_10_1016_j_marpolbul_2024_116284 |
| Cites_doi | 10.1016/S0022-2836(75)80111-2 10.1016/S0091-679X(06)80019-1 10.1038/293411a0 10.1007/s00018-014-1643-y 10.1080/07391102.2012.742460 10.1016/j.jinorgbio.2006.01.033 10.1126/science.1106653 10.3109/14756369609030310 10.1016/S0021-9258(17)44492-9 10.1038/218243a0 10.1016/j.pbiomolbio.2016.09.013 10.1182/blood.V84.1.325.325 10.1016/0022-2836(81)90254-0 10.1074/jbc.M508009200 10.1007/BF02783056 10.1016/j.mrrev.2013.08.002 10.1016/0141-8130(88)90014-1 10.1016/S0079-6107(98)00058-3 10.1007/BF02867412 10.1016/j.jinorgbio.2010.02.006 10.1021/jp4123425 10.1016/S0021-9258(17)40292-4 10.1016/S0140-6736(00)03238-4 10.1002/jmr.2648 10.1126/science.11.279.701 10.1074/jbc.M413317200 10.1126/science.87.2256.284 10.1016/S0167-4838(99)00021-7 10.1080/10715760701482451 10.1074/jbc.M406374200 10.1097/MD.0000000000000679 10.1074/jbc.M808106200 10.1016/0040-6031(89)87090-X 10.1107/S0907444910012321 10.1016/S0009-9120(01)00284-3 10.1016/j.electacta.2013.09.100 10.1016/j.jphotobiol.2013.08.006 10.1126/science.94.2452.615 10.1016/j.tibs.2006.11.003 10.1172/JCI104075 10.1016/S0140-6736(13)62365-X 10.1016/j.saa.2012.10.039 10.1073/pnas.052564899 10.1016/S0021-9258(19)50881-X 10.2116/analsci.28.711 10.1089/ars.2005.7.619 10.1111/j.1749-6632.1994.tb12073.x 10.1186/1471-2105-8-316 10.1016/0167-4838(87)90151-8 10.1038/nrd3054 10.1016/j.freeradbiomed.2015.05.018 10.1074/jbc.C300048200 10.1152/physrev.00010.2014 10.1016/0167-4838(95)00123-C 10.1093/nar/gkv951 10.1016/S1074-5521(02)00149-7 10.1007/s11357-006-9010-z 10.1042/bj3200061 10.1016/S0021-9258(18)47977-X 10.1016/S0940-2993(96)80055-8 10.1111/j.1440-1681.2007.04540.x 10.1161/01.RES.0000149564.49410.0d 10.1016/0014-5793(95)00568-T 10.1042/bst0290099 10.1038/srep46696 10.1016/j.abb.2017.06.018 10.1016/S0076-6879(84)05016-3 10.1016/0005-2744(67)90124-6 10.1073/pnas.73.6.2043 10.1016/S0898-8838(00)51001-0 10.1107/S0907444999007052 10.1073/pnas.0608407104 10.1016/0891-5849(94)90079-5 10.1006/abbi.1993.1036 10.1002/bit.260140205 10.1110/ps.0201402 10.1021/acs.biochem.6b01276 10.1016/0141-8130(87)90003-1 10.1093/clinchem/41.11.1574 10.1016/j.abb.2012.06.010 10.1152/ajprenal.00405.2012 10.1016/0040-6031(91)87116-E 10.1126/science.85.2206.366 10.1016/j.jbiotec.2014.03.002 10.1016/0003-2697(90)90026-6 10.1081/RRS-120037896 10.15430/JCP.2016.21.4.257 10.1515/hsz-2017-0131 10.1111/j.1530-0277.1995.tb01586.x 10.1021/bp034040t 10.1016/0003-2697(77)90662-5 10.1007/s00018-003-3206-5 10.1016/j.bbabio.2008.04.021 10.1016/0141-8130(89)90035-4 10.1021/bi00514a017 10.1002/mrd.1006 10.1073/pnas.78.8.4767 10.1016/j.transproceed.2005.11.083 10.1039/C3CC47022A 10.1016/j.ijbiomac.2013.03.070 10.1089/ars.2006.8.243 10.1073/pnas.82.6.1604 10.1007/s10067-007-0746-3 10.1016/j.ijbiomac.2016.11.050 10.1016/j.jinorgbio.2017.02.023 10.1111/j.1432-1033.1983.tb07429.x 10.1016/j.canlet.2006.10.029 10.1021/ja4075776 10.1021/bi061519w 10.1126/science.279.5347.98 10.1016/j.lfs.2007.01.028 10.1016/j.ijpharm.2015.04.078 10.3109/02713688709044503 10.1016/j.drudis.2008.07.005 10.1038/sj.ki.5002188 10.3109/10715762.2014.953139 10.1007/s11356-009-0112-x 10.1074/jbc.M404800200 |
| ContentType | Journal Article |
| Copyright | 2018 Elsevier Ltd Copyright © 2018 Elsevier Ltd. All rights reserved. |
| Copyright_xml | – notice: 2018 Elsevier Ltd – notice: Copyright © 2018 Elsevier Ltd. All rights reserved. |
| DBID | AAYXX CITATION NPM 7X8 |
| DOI | 10.1016/j.pbiomolbio.2018.03.001 |
| DatabaseName | CrossRef PubMed MEDLINE - Academic |
| DatabaseTitle | CrossRef PubMed MEDLINE - Academic |
| DatabaseTitleList | PubMed MEDLINE - Academic |
| Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Biology |
| EISSN | 1873-1732 |
| EndPage | 12 |
| ExternalDocumentID | 29530789 10_1016_j_pbiomolbio_2018_03_001 S0079610717302936 |
| Genre | Journal Article Review |
| GroupedDBID | --- --K --M -~X .GJ .~1 0R~ 123 1B1 1RT 1~. 1~5 29P 3O- 4.4 457 4G. 53G 5RE 5VS 7-5 71M 8P~ 9JM AACTN AAEDT AAEDW AAIAV AAIKJ AAKOC AALRI AAOAW AAQFI AAQXK AAXUO ABEFU ABFNM ABFRF ABGSF ABJNI ABLJU ABMAC ABTAH ABUDA ABXDB ABYKQ ACDAQ ACGFO ACGFS ACIUM ACRLP ADBBV ADEZE ADMUD ADUVX AEBSH AEFWE AEHWI AEKER AENEX AFFNX AFKWA AFTJW AFXIZ AGHFR AGRDE AGUBO AGYEJ AHHHB AIEXJ AIKHN AITUG AJBFU AJOXV ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ ASPBG AVWKF AXJTR AZFZN BKOJK BLXMC CS3 DOVZS DU5 EBS EFJIC EFLBG EJD EO8 EO9 EP2 EP3 F20 F5P FDB FEDTE FGOYB FIRID FNPLU FYGXN G-2 G-Q G8K GBLVA HLW HVGLF HX~ HZ~ IHE J1W KOM LX3 M41 MO0 MVM N9A O-L O9- OAUVE OZT P-8 P-9 P2P PC. Q38 R2- RIG ROL RPZ SBG SDF SDG SDP SES SEW SPCBC SPD SSU SSZ T5K UNMZH UQL VQP WUQ XFK ZGI ZY4 ~G- AATTM AAXKI AAYWO AAYXX ABDPE ABWVN ACRPL ACVFH ADCNI ADNMO ADVLN AEIPS AEUPX AFJKZ AFPUW AGCQF AGQPQ AGRNS AIGII AIIUN AKBMS AKRWK AKYEP ANKPU APXCP BNPGV CITATION SSH EFKBS NPM 7X8 |
| ID | FETCH-LOGICAL-c374t-c5f5aab58dd91afcba1a6f7241c05ae462442d708fe700413501d68acf39a0dc3 |
| IEDL.DBID | .~1 |
| ISSN | 0079-6107 1873-1732 |
| IngestDate | Fri Jul 11 08:58:41 EDT 2025 Mon Jul 21 05:46:04 EDT 2025 Tue Jul 01 00:42:39 EDT 2025 Thu Apr 24 23:00:00 EDT 2025 Fri Feb 23 02:29:20 EST 2024 |
| IsPeerReviewed | true |
| IsScholarly | true |
| Keywords | Thermodynamics Catalase Activity Mysteries Biophysical chemistry Kinetics Structure |
| Language | English |
| License | Copyright © 2018 Elsevier Ltd. All rights reserved. |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c374t-c5f5aab58dd91afcba1a6f7241c05ae462442d708fe700413501d68acf39a0dc3 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 ObjectType-Review-3 content type line 23 |
| PMID | 29530789 |
| PQID | 2013519699 |
| PQPubID | 23479 |
| PageCount | 8 |
| ParticipantIDs | proquest_miscellaneous_2013519699 pubmed_primary_29530789 crossref_citationtrail_10_1016_j_pbiomolbio_2018_03_001 crossref_primary_10_1016_j_pbiomolbio_2018_03_001 elsevier_sciencedirect_doi_10_1016_j_pbiomolbio_2018_03_001 |
| ProviderPackageCode | CITATION AAYXX |
| PublicationCentury | 2000 |
| PublicationDate | December 2018 2018-12-00 2018-Dec 20181201 |
| PublicationDateYYYYMMDD | 2018-12-01 |
| PublicationDate_xml | – month: 12 year: 2018 text: December 2018 |
| PublicationDecade | 2010 |
| PublicationPlace | England |
| PublicationPlace_xml | – name: England |
| PublicationTitle | Progress in biophysics and molecular biology |
| PublicationTitleAlternate | Prog Biophys Mol Biol |
| PublicationYear | 2018 |
| Publisher | Elsevier Ltd |
| Publisher_xml | – name: Elsevier Ltd |
| References | Schriner, Linford (bib101) 2006; 28 Hong, Wang, Huang, Yang, Zhao, Xiao, Gao, Moosavi-Movahedi, Ghourchian, Moosavi-Movahedi (bib40) 2012; 28 Yang, Hao, Li, Chen, Liu (bib130) 2013; 128 Loew (bib65) 1900; 11 Moosavi Movahedi, Nazari, Ghadermarzi (bib77) 1999; 48 Stone, Yang (bib110) 2006; 8 Sumner, Dounce (bib112) 1937; 85 Smulevich, Jakopitsch, Droghetti, Obinger (bib108) 2006; 100 Moosavi-Movahedi, Ghobadi (bib73) 1991; 189 Takahara, Hamilton, Neel, Kobara, Ogura, Nishimura (bib115) 1960; 39 Vives-Bauza, Starkov, Garcia-Arumi (bib125) 2007; 80 Ho, Xiong, Ma, Spector, Ho (bib38) 2004; 279 Laskowski, Sumner (bib61) 1941; 94 O'Neill (bib83) 1972; 14 Moosavi-Movahedi, Pilcher, Jones (bib78) 1989; 146 Pichorner, Jessner, Ebermann (bib88) 1993; 300 Nicholls, Fita, Loewen (bib82) 2000; 51 López-Lázaro (bib66) 2007; 252 Rorth, Jensen (bib95) 1967; 139 Shi, Lo, Chenier, Maachi, Filep, Ingelfinger, Zhang, Chan (bib105) 2013; 304 Suarez, Ranguelova, Jarzecki, Manzerova, Krymov, Zhao, Yu, Metlitsky, Gerfen, Magliozzo (bib111) 2009; 284 Brezniceanu, Liu, Wei, Tran, Sachetelli, Zhang, Guo, Filep, Ingelfinger, Chan (bib10) 2007; 71 Wu, Li, Du, Li, Ren (bib129) 2007; 34 Kalpakcioglu, Senel (bib48) 2008; 27 Ivancich, Loewen (bib41) 2013 Rozwarski, Grant, Barton, Jacobs, Sacchettini (bib98) 1998; 279 Jemec, Drobne, Tisler, Sepcic (bib45) 2010; 17 Jones, Finn, Moosavi-Movahedi, Waller (bib47) 1987; 913 Liu, Eisenberg (bib64) 2002; 11 Yang, Roberts, Shi, Zhou, Ballard, Richardson, Guo (bib131) 2004; 95 Özmen, Özmen, Erkin, Güner, Habif, Bayındır (bib86) 2002; 35 Vainshtein, Melik-Adamyan, Barynin, Vagin, Grebenko (bib121) 1981; 293 Lei, Zhu, Cheng, Bao, Ho, Reddi, Holmgren, Arnér (bib63) 2016; 96 Kitani, Kanai, Carrillo, Ivy (bib52) 1994; 717 Michiels, Raes, Toussaint, Remacle (bib70) 1994; 17 Thompson, Schaller, Apel (bib118) 2003; 19 Chang, Poznansky (bib11) 1968; 218 Hanwell, Curtis, Lonie, Vandermeersch, Zurek, Hutchison (bib34) 2012; 4 Krych-Madej, Gebicka (bib57) 2017; 171 Unwin (bib120) 1975; 98 Krych, Gebicka (bib58) 2013; 58 Cornish-Bowden (bib16) 2016, Garland Science Shen, Li, Tian, Shen, Zhu, Feng, Wan, Yang, Chen, Wen (bib104) 2015; 94 Del Rio, Ortega, Lopez, Gorge (bib19) 1977; 80 Vidossich, Loewen, Carpena, Fiorin, Fita, Rovira (bib124) 2014; 118 Jha, Chelikani, Carpena, Fita, Loewen (bib46) 2012; 526 Moosavi-Movahedi, Jones, Pilcher (bib76) 1989; 11 Goth, Nagy (bib32) 2013; 753 Fita, Rossmann (bib24) 1985; 82 Murthy, Reid, Sicignano, Tanaka, Rossmann (bib81) 1981; 152 Bicout, Field, Gouet, Jouve (bib7) 1995; 1252 DeJong, Miller, Molina-Cruz, Gupta, Kumar, Barillas-Mury (bib18) 2007; 104 Holdgate, Fisher, Ward (bib39) 2004 Martinelli, Rotta, Villela, Rodrigues-Junior, Abbadi, Trindade, Petersen, Danesi, Nery, Pauli, Campos, Bonan, de Souza, Basso, Santos (bib68) 2017; 7 Lazarow, De Duve (bib62) 1976; 73 Bisswanger (bib8) 2017 Jakopitsch, Droghetti, Schmuckenschlager, Furtmuller, Smulevich, Obinger (bib43) 2005; 280 Siddiqui, Ertan, Charlton, Poljak, Daud Khaled, Yang, Marshall, Cavicchioli (bib106) 2014; 178 Porter, Bright (bib90) 1987; 262 Zamocky, Herzog, Nykyri, Koller (bib136) 1995; 367 Sepasi Tehrani, Moosavi-Movahedi, Ghourchian, Ahmad, Kiany, Atri, Ariaeenejad, Kavousi, Saboury (bib103) 2013; 31 Vlasits, Bellei, Jakopitsch, De Rienzo, Furtmuller, Zamocky, Sola, Battistuzzi, Obinger (bib126) 2010; 104 Mofidi Najjar, Taghavi, Ghadari, Sheibani, Moosavi-Movahedi (bib72) 2017; 630 Yekta, Dehghan, Rashtbari, Sheibani, Moosavi-Movahedi (bib134) 2017; 30 Hertz, Russell (bib37) 2007 Porollo, Meller (bib89) 2007; 8 Schaefer, Lee (bib99) 2015; 489 Chelikani, Fita, Loewen (bib13) 2004; 61 Jakopitsch, Wanasinghe, Jantschko, Furtmuller, Obinger (bib44) 2005; 280 Zámocký, Koller (bib137) 1999; 72 Aebi (bib2) 1984; 105 Mofidi Najjar, Ghadari, Yousefi, Safari, Sheikhhasani, Sheibani, Moosavi-Movahedi (bib71) 2017; 95 Heck, Vetrano, Mariano, Laskin (bib36) 2003; 278 Moosavi-Movahedi, Wilkinson, Jones (bib75) 1987; 9 Izawa, Inoue, Kimura (bib42) 1996; 320 Aehle (bib3) 2007 Takahara, Miyamoto (bib116) 1948; 51 Breiten, Lockett, Sherman, Fujita, Al-Sayah, Lange, Bowers, Heroux, Krilov, Whitesides (bib9) 2013; 135 Freire (bib25) 2008; 13 Ladbury, Klebe, Freire (bib60) 2010; 9 Sepasi Tehrani, Moosavi-Movahedi, Ghourchian (bib117) 2013; 113 Khan, Zaman, Chandel, Siddiqui, Ajmal, Abdelhameed, Khan (bib49) 2017 Banerjee, Becker, Dickman, Gladyshev, Ragsdale (bib5) 2007 Ghadermarzi, Moosavi-Movahedi (bib28) 1999; 1431 Regelsberger, Jakopitsch, Furtmuller, Rueker, Switala, Loewen, Obinger (bib92) 2001; 29 Wang, Zhang, Wang, Dou, Li, Wang, Pu, Wang (bib127) 2013; 102 Klinger, Karge, Kretzschmar, Rost, Schulze, Dargel, Reinemann, Rein (bib53) 1996; 48 Rousseau, Schymkowitz, Itzhaki (bib97) 2012 Chelikani, Ramana, Radhakrishnan (bib14) 2005; 20 Sykes, Mauk (bib114) 2000 Copeland (bib15) 2013 Ghadermarzi, Moosavi-Movahedi (bib27) 1996; 10 Krych, Gebicki, Gebicka (bib59) 2014; 48 Zamocky, Gasselhuber, Furtmuller, Obinger (bib135) 2014; 71 Valderrama, Ayala, Vazquez-Duhalt (bib122) 2002; 9 Yasmineh, Kaur, Blazar, Theologides (bib133) 1995; 41 Perozzo, Folkers, Scapozza (bib87) 2004; 24 Rhee, Yang, Kang, Woo, Chang (bib94) 2005; 7 Kirkman, Gaetani (bib51) 2007; 32 Ko, Day, Malkin, McPherson (bib54) 1999; 55 Machuqueiro, Victor, Switala, Villanueva, Rovira, Fita, Loewen (bib67) 2017; 56 Domański, L., Safranow, K., Dołȩgowska, B., Różański, J., Myślak, M., Ciechanowski, K., Jakubowska, K., Dziedziejko, V., Romanowski, M., Sulikowski, T., Sieńko, J., Kamiński, M., Ostrowski, M., Domański, M., Pawlik, A., Rać, M.E. and Chlubek, D. Hypoxanthine as a graft ischemia marker stimulates catalase activity in the renal vein during reperfusion in humans, Transplantation Proceedings. 38, 35–38. Koechling, Amit, Negrete (bib55) 1995; 19 Moser, Chobot, Page, Dutton (bib79) 2008; 1777 Hara, Ichise, Kojima, Kondo, Ohgiya, Matsuyama, Yumoto (bib35) 2007; 46 Moosavi-Movahedi, Jones, Pilcher (bib74) 1988; 10 Csukas, Costarides, Riley, Green (bib17) 1987; 6 Abuchowski, McCoy, Palczuk, van Es, Davis (bib1) 1977; 252 Goth, Eaton (bib31) 2000; 356 Schallreuter, Elwary (bib100) 2007; 80 Reid, Murthy, Sicignano, Tanaka, Musick, Rossmann (bib93) 1981; 78 Góth, Bigler (bib30) 2007; 41 Ortiz de Montellano, Kerr (bib85) 1983; 258 Zhang, Piao, Oh, Park, Shilnikova, Moon, Kim, Jung, Kim, Hyun (bib138) 2016; 21 Ross, Subramanian (bib96) 1981; 20 Schriner, Linford, Martin, Treuting, Ogburn, Emond, Coskun, Ladiges, Wolf, Van Remmen (bib102) 2005; 308 Escobar, Salvador, Contreras, Escamilla (bib23) 1990; 184 Tovmasyan, Maia, Weitner, Carballal, Sampaio, Lieb, Ghazaryan, Ivanovic-Burmazovic, Ferrer-Sueta, Radi (bib119) 2015; 86 Beers, Sizer (bib6) 1952; 195 Cheetham (bib12) 2011 Singh, Wiseman, Deemagarn, Donald, Duckworth, Carpena, Fita, Loewen (bib107) 2004; 279 Kim, Thiessen, Bolton, Chen, Fu, Gindulyte, Han, He, He, Shoemaker, Wang, Yu, Zhang, Bryant (bib50) 2016; 44 Murakami, Fukushima, Ishikawa, Yamazaki (bib80) 1984; 33 Orsi, Leese (bib84) 2001; 59 Dunford (bib21) 2010 Krumova, Cosa (bib56) 2016 Watson (bib128) 2014; 383 Sumner, Gralen (bib113) 1938; 87 Hamada, Kameyama, Iizuka, Ishizaki, Nishiyama, Isshiki (bib33) 2004; 101 Potapovich, Eremin, Metelitsa (bib91) 2003; 39 Glorieux, Calderon (bib29) 2017; 398 Epp, Ladenstein, Wendel (bib22) 1983; 133 Starr, Taggart (bib109) 2005 Mascarenhas, Gosavi (bib69) 2017; 128 Ascone, Savino, Kahn, Fourme (bib4) 2010; 66 Gaetani, Kirkman, Mangerini, Ferraris (bib26) 1994; 84 Zhao, Hersleth, Zhu, Andersson, Magliozzo (bib139) 2013; 49 Yang, Poovaiah (bib132) 2002; 99 Vasudevan, Thakur (bib123) 1994; 49 Aehle (10.1016/j.pbiomolbio.2018.03.001_bib3) 2007 Yekta (10.1016/j.pbiomolbio.2018.03.001_bib134) 2017; 30 Chelikani (10.1016/j.pbiomolbio.2018.03.001_bib13) 2004; 61 Ko (10.1016/j.pbiomolbio.2018.03.001_bib54) 1999; 55 Jakopitsch (10.1016/j.pbiomolbio.2018.03.001_bib44) 2005; 280 Ross (10.1016/j.pbiomolbio.2018.03.001_bib96) 1981; 20 Wang (10.1016/j.pbiomolbio.2018.03.001_bib127) 2013; 102 Machuqueiro (10.1016/j.pbiomolbio.2018.03.001_bib67) 2017; 56 Murthy (10.1016/j.pbiomolbio.2018.03.001_bib81) 1981; 152 Rhee (10.1016/j.pbiomolbio.2018.03.001_bib94) 2005; 7 Rorth (10.1016/j.pbiomolbio.2018.03.001_bib95) 1967; 139 Breiten (10.1016/j.pbiomolbio.2018.03.001_bib9) 2013; 135 Hong (10.1016/j.pbiomolbio.2018.03.001_bib40) 2012; 28 Góth (10.1016/j.pbiomolbio.2018.03.001_bib30) 2007; 41 Ladbury (10.1016/j.pbiomolbio.2018.03.001_bib60) 2010; 9 Rozwarski (10.1016/j.pbiomolbio.2018.03.001_bib98) 1998; 279 Potapovich (10.1016/j.pbiomolbio.2018.03.001_bib91) 2003; 39 Moosavi-Movahedi (10.1016/j.pbiomolbio.2018.03.001_bib73) 1991; 189 Vlasits (10.1016/j.pbiomolbio.2018.03.001_bib126) 2010; 104 Ghadermarzi (10.1016/j.pbiomolbio.2018.03.001_bib27) 1996; 10 Krumova (10.1016/j.pbiomolbio.2018.03.001_bib56) 2016 Moosavi Movahedi (10.1016/j.pbiomolbio.2018.03.001_bib77) 1999; 48 Laskowski (10.1016/j.pbiomolbio.2018.03.001_bib61) 1941; 94 Fita (10.1016/j.pbiomolbio.2018.03.001_bib24) 1985; 82 Michiels (10.1016/j.pbiomolbio.2018.03.001_bib70) 1994; 17 Glorieux (10.1016/j.pbiomolbio.2018.03.001_bib29) 2017; 398 Moosavi-Movahedi (10.1016/j.pbiomolbio.2018.03.001_bib78) 1989; 146 Hanwell (10.1016/j.pbiomolbio.2018.03.001_bib34) 2012; 4 Koechling (10.1016/j.pbiomolbio.2018.03.001_bib55) 1995; 19 Tovmasyan (10.1016/j.pbiomolbio.2018.03.001_bib119) 2015; 86 Valderrama (10.1016/j.pbiomolbio.2018.03.001_bib122) 2002; 9 Yang (10.1016/j.pbiomolbio.2018.03.001_bib130) 2013; 128 Sepasi Tehrani (10.1016/j.pbiomolbio.2018.03.001_bib103) 2013; 31 Brezniceanu (10.1016/j.pbiomolbio.2018.03.001_bib10) 2007; 71 Unwin (10.1016/j.pbiomolbio.2018.03.001_bib120) 1975; 98 Nicholls (10.1016/j.pbiomolbio.2018.03.001_bib82) 2000; 51 Vives-Bauza (10.1016/j.pbiomolbio.2018.03.001_bib125) 2007; 80 Bicout (10.1016/j.pbiomolbio.2018.03.001_bib7) 1995; 1252 Chelikani (10.1016/j.pbiomolbio.2018.03.001_bib14) 2005; 20 Hamada (10.1016/j.pbiomolbio.2018.03.001_bib33) 2004; 101 Goth (10.1016/j.pbiomolbio.2018.03.001_bib31) 2000; 356 Smulevich (10.1016/j.pbiomolbio.2018.03.001_bib108) 2006; 100 Dunford (10.1016/j.pbiomolbio.2018.03.001_bib21) 2010 Zamocky (10.1016/j.pbiomolbio.2018.03.001_bib135) 2014; 71 Bisswanger (10.1016/j.pbiomolbio.2018.03.001_bib8) 2017 Ivancich (10.1016/j.pbiomolbio.2018.03.001_bib41) 2013 Perozzo (10.1016/j.pbiomolbio.2018.03.001_bib87) 2004; 24 Moosavi-Movahedi (10.1016/j.pbiomolbio.2018.03.001_bib74) 1988; 10 Escobar (10.1016/j.pbiomolbio.2018.03.001_bib23) 1990; 184 Schallreuter (10.1016/j.pbiomolbio.2018.03.001_bib100) 2007; 80 Siddiqui (10.1016/j.pbiomolbio.2018.03.001_bib106) 2014; 178 Banerjee (10.1016/j.pbiomolbio.2018.03.001_bib5) 2007 Pichorner (10.1016/j.pbiomolbio.2018.03.001_bib88) 1993; 300 Hertz (10.1016/j.pbiomolbio.2018.03.001_bib37) 2007 López-Lázaro (10.1016/j.pbiomolbio.2018.03.001_bib66) 2007; 252 Reid (10.1016/j.pbiomolbio.2018.03.001_bib93) 1981; 78 Orsi (10.1016/j.pbiomolbio.2018.03.001_bib84) 2001; 59 Vasudevan (10.1016/j.pbiomolbio.2018.03.001_bib123) 1994; 49 Stone (10.1016/j.pbiomolbio.2018.03.001_bib110) 2006; 8 Martinelli (10.1016/j.pbiomolbio.2018.03.001_bib68) 2017; 7 Heck (10.1016/j.pbiomolbio.2018.03.001_bib36) 2003; 278 Holdgate (10.1016/j.pbiomolbio.2018.03.001_bib39) 2004 Goth (10.1016/j.pbiomolbio.2018.03.001_bib32) 2013; 753 Suarez (10.1016/j.pbiomolbio.2018.03.001_bib111) 2009; 284 Porollo (10.1016/j.pbiomolbio.2018.03.001_bib89) 2007; 8 Sumner (10.1016/j.pbiomolbio.2018.03.001_bib112) 1937; 85 Moser (10.1016/j.pbiomolbio.2018.03.001_bib79) 2008; 1777 Wu (10.1016/j.pbiomolbio.2018.03.001_bib129) 2007; 34 Ho (10.1016/j.pbiomolbio.2018.03.001_bib38) 2004; 279 Freire (10.1016/j.pbiomolbio.2018.03.001_bib25) 2008; 13 Moosavi-Movahedi (10.1016/j.pbiomolbio.2018.03.001_bib76) 1989; 11 Beers (10.1016/j.pbiomolbio.2018.03.001_bib6) 1952; 195 Takahara (10.1016/j.pbiomolbio.2018.03.001_bib116) 1948; 51 Chang (10.1016/j.pbiomolbio.2018.03.001_bib11) 1968; 218 Jemec (10.1016/j.pbiomolbio.2018.03.001_bib45) 2010; 17 Vainshtein (10.1016/j.pbiomolbio.2018.03.001_bib121) 1981; 293 Rousseau (10.1016/j.pbiomolbio.2018.03.001_bib97) 2012 Watson (10.1016/j.pbiomolbio.2018.03.001_bib128) 2014; 383 Yang (10.1016/j.pbiomolbio.2018.03.001_bib131) 2004; 95 Krych (10.1016/j.pbiomolbio.2018.03.001_bib58) 2013; 58 Abuchowski (10.1016/j.pbiomolbio.2018.03.001_bib1) 1977; 252 Kim (10.1016/j.pbiomolbio.2018.03.001_bib50) 2016; 44 Zámocký (10.1016/j.pbiomolbio.2018.03.001_bib137) 1999; 72 Zhao (10.1016/j.pbiomolbio.2018.03.001_bib139) 2013; 49 Kirkman (10.1016/j.pbiomolbio.2018.03.001_bib51) 2007; 32 Porter (10.1016/j.pbiomolbio.2018.03.001_bib90) 1987; 262 Starr (10.1016/j.pbiomolbio.2018.03.001_bib109) 2005 Kitani (10.1016/j.pbiomolbio.2018.03.001_bib52) 1994; 717 Liu (10.1016/j.pbiomolbio.2018.03.001_bib64) 2002; 11 O'Neill (10.1016/j.pbiomolbio.2018.03.001_bib83) 1972; 14 Yang (10.1016/j.pbiomolbio.2018.03.001_bib132) 2002; 99 Csukas (10.1016/j.pbiomolbio.2018.03.001_bib17) 1987; 6 Khan (10.1016/j.pbiomolbio.2018.03.001_bib49) 2017 Loew (10.1016/j.pbiomolbio.2018.03.001_bib65) 1900; 11 Gaetani (10.1016/j.pbiomolbio.2018.03.001_bib26) 1994; 84 Moosavi-Movahedi (10.1016/j.pbiomolbio.2018.03.001_bib75) 1987; 9 Ortiz de Montellano (10.1016/j.pbiomolbio.2018.03.001_bib85) 1983; 258 Zhang (10.1016/j.pbiomolbio.2018.03.001_bib138) 2016; 21 Sepasi Tehrani (10.1016/j.pbiomolbio.2018.03.001_bib117) 2013; 113 Krych-Madej (10.1016/j.pbiomolbio.2018.03.001_bib57) 2017; 171 Sykes (10.1016/j.pbiomolbio.2018.03.001_bib114) 2000 Schaefer (10.1016/j.pbiomolbio.2018.03.001_bib99) 2015; 489 Mofidi Najjar (10.1016/j.pbiomolbio.2018.03.001_bib71) 2017; 95 Copeland (10.1016/j.pbiomolbio.2018.03.001_bib15) 2013 Mofidi Najjar (10.1016/j.pbiomolbio.2018.03.001_bib72) 2017; 630 Sumner (10.1016/j.pbiomolbio.2018.03.001_bib113) 1938; 87 Mascarenhas (10.1016/j.pbiomolbio.2018.03.001_bib69) 2017; 128 Shi (10.1016/j.pbiomolbio.2018.03.001_bib105) 2013; 304 Takahara (10.1016/j.pbiomolbio.2018.03.001_bib115) 1960; 39 Schriner (10.1016/j.pbiomolbio.2018.03.001_bib102) 2005; 308 Schriner (10.1016/j.pbiomolbio.2018.03.001_bib101) 2006; 28 Cheetham (10.1016/j.pbiomolbio.2018.03.001_bib12) 2011 Zamocky (10.1016/j.pbiomolbio.2018.03.001_bib136) 1995; 367 Lazarow (10.1016/j.pbiomolbio.2018.03.001_bib62) 1976; 73 Del Rio (10.1016/j.pbiomolbio.2018.03.001_bib19) 1977; 80 Thompson (10.1016/j.pbiomolbio.2018.03.001_bib118) 2003; 19 Vidossich (10.1016/j.pbiomolbio.2018.03.001_bib124) 2014; 118 Regelsberger (10.1016/j.pbiomolbio.2018.03.001_bib92) 2001; 29 Lei (10.1016/j.pbiomolbio.2018.03.001_bib63) 2016; 96 Jakopitsch (10.1016/j.pbiomolbio.2018.03.001_bib43) 2005; 280 Ghadermarzi (10.1016/j.pbiomolbio.2018.03.001_bib28) 1999; 1431 Cornish-Bowden (10.1016/j.pbiomolbio.2018.03.001_bib16) 2016 Jones (10.1016/j.pbiomolbio.2018.03.001_bib47) 1987; 913 Hara (10.1016/j.pbiomolbio.2018.03.001_bib35) 2007; 46 Jha (10.1016/j.pbiomolbio.2018.03.001_bib46) 2012; 526 Izawa (10.1016/j.pbiomolbio.2018.03.001_bib42) 1996; 320 Ascone (10.1016/j.pbiomolbio.2018.03.001_bib4) 2010; 66 Epp (10.1016/j.pbiomolbio.2018.03.001_bib22) 1983; 133 Singh (10.1016/j.pbiomolbio.2018.03.001_bib107) 2004; 279 Yasmineh (10.1016/j.pbiomolbio.2018.03.001_bib133) 1995; 41 Klinger (10.1016/j.pbiomolbio.2018.03.001_bib53) 1996; 48 Shen (10.1016/j.pbiomolbio.2018.03.001_bib104) 2015; 94 Özmen (10.1016/j.pbiomolbio.2018.03.001_bib86) 2002; 35 DeJong (10.1016/j.pbiomolbio.2018.03.001_bib18) 2007; 104 10.1016/j.pbiomolbio.2018.03.001_bib20 Murakami (10.1016/j.pbiomolbio.2018.03.001_bib80) 1984; 33 Kalpakcioglu (10.1016/j.pbiomolbio.2018.03.001_bib48) 2008; 27 Krych (10.1016/j.pbiomolbio.2018.03.001_bib59) 2014; 48 Aebi (10.1016/j.pbiomolbio.2018.03.001_bib2) 1984; 105 |
| References_xml | – volume: 280 start-page: 42411 year: 2005 end-page: 42422 ident: bib43 article-title: Role of the main access channel of catalase-peroxidase in catalysis publication-title: J. Biol. Chem. – volume: 34 start-page: 81 year: 2007 end-page: 87 ident: bib129 article-title: Cardiac-specific overexpression of catalase prolongs lifespan and attenuates ageing-induced cardiomyocyte contractile dysfunction and protein damage publication-title: Clin. Exp. Pharmacol. Physiol. – volume: 9 start-page: 23 year: 2010 end-page: 27 ident: bib60 article-title: Adding calorimetric data to decision making in lead discovery: a hot tip publication-title: Nat. Rev. Drug Discov. – volume: 218 start-page: 243 year: 1968 end-page: 245 ident: bib11 article-title: Semipermeable microcapsules containing catalase for enzyme replacement in acatalasaemic mice publication-title: Nature – start-page: 1 year: 2017 end-page: 15 ident: bib49 article-title: Cationic surfactant mediated fibrillogenesis in bovine liver catalase: a biophysical approach publication-title: J. Biomol. Struct. Dyn. – volume: 526 start-page: 54 year: 2012 end-page: 59 ident: bib46 article-title: Influence of main channel structure on H publication-title: Arch. Biochem. Biophys. – volume: 98 start-page: 235 year: 1975 end-page: 242 ident: bib120 article-title: Beef liver catalase structure: interpretation of electron micrographs publication-title: J. Mol. Biol. – volume: 1431 start-page: 30 year: 1999 end-page: 36 ident: bib28 article-title: Influence of different types of effectors on the kinetic parameters of suicide inactivation of catalase by hydrogen peroxide publication-title: Biochim. Biophys. Acta – volume: 367 start-page: 241 year: 1995 end-page: 245 ident: bib136 article-title: Site-directed mutagenesis of the lower parts of the major substrate channel of yeast catalase A leads to highly increased peroxidatic activity publication-title: FEBS Lett. – year: 2004 ident: bib39 article-title: The Application of Isothermal Titration Calorimetry to Drug Discovery – volume: 146 start-page: 215 year: 1989 end-page: 223 ident: bib78 article-title: Thermodynamics of the interaction between n-dodecyltrimethylammonium bromide and catalases publication-title: Thermochim. Acta – volume: 56 start-page: 2271 year: 2017 end-page: 2281 ident: bib67 article-title: The catalase activity of catalase-peroxidases is modulated by changes in the pKa of the distal histidine publication-title: Biochemistry – volume: 1252 start-page: 172 year: 1995 end-page: 176 ident: bib7 article-title: Simulations of electron transfer in the NADPH-bound catalase from Proteus mirabilis PR publication-title: Biochim. Biophys. Acta – year: 2005 ident: bib109 article-title: Biology: the Unity and Diversity of Life – volume: 278 start-page: 22432 year: 2003 end-page: 22436 ident: bib36 article-title: UVB light stimulates production of reactive oxygen species: unexpected role for catalase publication-title: J. Biol. Chem. – volume: 84 start-page: 325 year: 1994 end-page: 330 ident: bib26 article-title: Importance of catalase in the disposal of hydrogen peroxide within human erythrocytes publication-title: Blood – volume: 300 start-page: 258 year: 1993 end-page: 264 ident: bib88 article-title: tBOOH acts as a suicide substrate for catalase publication-title: Arch. Biochem. Biophys. – volume: 105 start-page: 121 year: 1984 end-page: 126 ident: bib2 article-title: Catalase in vitro publication-title: Methods Enzymol. – volume: 128 start-page: 113 year: 2017 end-page: 120 ident: bib69 article-title: Understanding protein domain-swapping using structure-based models of protein folding publication-title: Prog. Biophys. Mol. Biol. – volume: 51 start-page: 51 year: 2000 end-page: 106 ident: bib82 article-title: Enzymology and structure of catalases publication-title: Adv. Inorg. Chem. – volume: 178 start-page: 1 year: 2014 end-page: 11 ident: bib106 article-title: Versatile peroxidase degradation of humic substances: use of isothermal titration calorimetry to assess kinetics, and applications to industrial wastes publication-title: J. Biotechnol. – volume: 48 start-page: 447 year: 1996 end-page: 460 ident: bib53 article-title: Luminol-and lucigenin-amplified chemiluminescence with rat liver microsomes. Kinetics and influence of ascorbic acid, glutathione, dimethylsulfoxide, N-t-butyl-a-phenyl-nitrone, copper-ions and a copper complex, catalase, superoxide dismutase, hexobarbital and aniline publication-title: Exp. Toxicol. Pathol. – volume: 94 start-page: 615 year: 1941 ident: bib61 article-title: Crystalline catalase from beef erythrocytes publication-title: Science – volume: 78 start-page: 4767 year: 1981 end-page: 4771 ident: bib93 article-title: Structure and heme environment of beef liver catalase at 2.5 A resolution publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 41 start-page: 953 year: 2007 end-page: 955 ident: bib30 article-title: Catalase deficiency may complicate urate oxidase (rasburicase) therapy publication-title: Free Radic. Res. – volume: 99 start-page: 4097 year: 2002 end-page: 4102 ident: bib132 article-title: Hydrogen peroxide homeostasis: activation of plant catalase by calcium/calmodulin publication-title: Proc. Natl. Acad. Sci. U. S. A. – year: 2007 ident: bib3 article-title: Enzymes in Industry: Production and Applications – start-page: 137 year: 2012 end-page: 152 ident: bib97 article-title: Implications of 3D Domain Swapping for Protein Folding, Misfolding and Function, Protein Dimerization and Oligomerization in Biology – year: 2016 ident: bib56 article-title: Overview of Reactive Oxygen Species – volume: 139 start-page: 171 year: 1967 end-page: 173 ident: bib95 article-title: Determination of catalase activity by means of the Clark oxygen electrode publication-title: Biochim. Biophys. Acta – volume: 102 start-page: 88 year: 2013 end-page: 98 ident: bib127 article-title: Spectroscopic study on the interaction of catalase with bifendate and analogs publication-title: Spectrochim. Acta Mol. Biomol. Spectrosc. – volume: 49 start-page: 11650 year: 2013 end-page: 11652 ident: bib139 article-title: Access channel residues Ser315 and Asp137 in Mycobacterium tuberculosis catalase-peroxidase (KatG) control peroxidatic activation of the pro-drug isoniazid publication-title: Chem. Commun. – year: 2011 ident: bib12 article-title: Introducing Biological Energetics: How Energy and Information Control the Living World – volume: 113 start-page: 591 year: 2013 end-page: 602 ident: bib117 article-title: Correlation between biological activity and electron transferring of bovine liver catalase: osmolytes effects publication-title: Electrochim. Acta – volume: 31 start-page: 1440 year: 2013 end-page: 1454 ident: bib103 article-title: Effect of compatible and noncompatible osmolytes on the enzymatic activity and thermal stability of bovine liver catalase publication-title: J. Biomol. Struct. Dyn. – volume: 46 start-page: 11 year: 2007 end-page: 22 ident: bib35 article-title: Relationship between the size of the bottleneck 15 A from iron in the main channel and the reactivity of catalase corresponding to the molecular size of substrates publication-title: Biochemistry – volume: 55 start-page: 1383 year: 1999 end-page: 1394 ident: bib54 article-title: Structure of orthorhombic crystals of beef liver catalase publication-title: Acta Crystallogr. Sect. D Biol. Crystallogr. – volume: 304 start-page: F1335 year: 2013 end-page: F1346 ident: bib105 article-title: Overexpression of catalase prevents hypertension and tubulointerstitial fibrosis and normalization of renal angiotensin-converting enzyme-2 expression in Akita mice publication-title: Am. J. Physiol. Ren. Physiol. – year: 2007 ident: bib37 article-title: General Biology – volume: 398 start-page: 1095 year: 2017 end-page: 1108 ident: bib29 article-title: Catalase, a remarkable enzyme: targeting the oldest antioxidant enzyme to find a new cancer treatment approach publication-title: Biol. Chem. – volume: 61 start-page: 192 year: 2004 end-page: 208 ident: bib13 article-title: Diversity of structures and properties among catalases publication-title: Cell. Mol. Life Sci. – volume: 101 start-page: 247 year: 2004 end-page: 248 ident: bib33 article-title: Methemoglobinemia from hydrogen peroxide in a patient with acatalasemia publication-title: J. Am. Soc. Anesthesiologists – volume: 104 start-page: 2121 year: 2007 end-page: 2126 ident: bib18 article-title: Reactive oxygen species detoxification by catalase is a major determinant of fecundity in the mosquito publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 28 start-page: 711 year: 2012 end-page: 716 ident: bib40 article-title: A highly efficient nano-cluster artificial peroxidase and its direct electrochemistry on a nano complex modified glassy carbon electrode publication-title: Anal. Sci. – year: 2017 ident: bib8 article-title: Enzyme Kinetics: Principles and Methods – volume: 32 start-page: 44 year: 2007 end-page: 50 ident: bib51 article-title: Mammalian catalase: a venerable enzyme with new mysteries publication-title: Trends Biochem. Sci. – volume: 80 start-page: 2221 year: 2007 end-page: 2226 ident: bib100 article-title: Hydrogen peroxide regulates the cholinergic signal in a concentration dependent manner publication-title: Life Sci. – volume: 59 start-page: 44 year: 2001 end-page: 53 ident: bib84 article-title: Protection against reactive oxygen species during mouse preimplantation embryo development: role of EDTA, oxygen tension, catalase, superoxide dismutase and pyruvate publication-title: Mol. Reprod. Dev. – volume: 39 start-page: 160 year: 2003 end-page: 166 ident: bib91 article-title: Kinetics of catalase inactivation induced by ultrasonic cavitation publication-title: Prikl. Biokhim. Mikrobiol. – start-page: 611 year: 2013 end-page: 614 ident: bib41 article-title: Electron transfer in catalases and catalase-peroxidases publication-title: Encyclopedia of Biophysics – volume: 195 start-page: 133 year: 1952 end-page: 140 ident: bib6 article-title: A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase publication-title: J. Biol. Chem. – volume: 10 start-page: 167 year: 1996 end-page: 175 ident: bib27 article-title: Determination of the kinetic parameters for the “suicide substrate” inactivation of bovine liver catalase by hydrogen peroxide publication-title: J. Enzym. Inhib. – volume: 48 start-page: 9 year: 1999 end-page: 17 ident: bib77 article-title: Suicide inactivation of peroxidase by H publication-title: Ital. J. Biochem. – volume: 71 start-page: 912 year: 2007 end-page: 923 ident: bib10 article-title: Catalase overexpression attenuates angiotensinogen expression and apoptosis in diabetic mice publication-title: Kidney Int. – volume: 17 start-page: 571 year: 2010 end-page: 581 ident: bib45 article-title: Biochemical biomarkers in environmental studies–lessons learnt from enzymes catalase, glutathione S-transferase and cholinesterase in two crustacean species publication-title: Environ. Sci. Pollut. Res. Int. – volume: 33 start-page: 401 year: 1984 end-page: 404 ident: bib80 article-title: Visualization of surface structure of catalase crystals by metal decoration publication-title: J. Electron. Microsc.(Tokyo) – volume: 95 start-page: 550 year: 2017 end-page: 556 ident: bib71 article-title: Studies to reveal the nature of interactions between catalase and curcumin using computational methods and optical techniques publication-title: Int. J. Biol. Macromol. – volume: 71 start-page: 4681 year: 2014 end-page: 4696 ident: bib135 article-title: Turning points in the evolution of peroxidase-catalase superfamily: molecular phylogeny of hybrid heme peroxidases publication-title: Cell. Mol. Life Sci. – volume: 20 start-page: 3096 year: 1981 end-page: 3102 ident: bib96 article-title: Thermodynamics of protein association reactions: forces contributing to stability publication-title: Biochemistry – volume: 66 start-page: 654 year: 2010 end-page: 663 ident: bib4 article-title: Flexibility of the Cu,Zn superoxide dismutase structure investigated at 0.57 GPa publication-title: Acta Crystallogr. Sect. D Biol. Crystallogr. – year: 2013 ident: bib15 article-title: Evaluation of Enzyme Inhibitors in Drug Discovery: a Guide for Medicinal Chemists and Pharmacologists – reference: Domański, L., Safranow, K., Dołȩgowska, B., Różański, J., Myślak, M., Ciechanowski, K., Jakubowska, K., Dziedziejko, V., Romanowski, M., Sulikowski, T., Sieńko, J., Kamiński, M., Ostrowski, M., Domański, M., Pawlik, A., Rać, M.E. and Chlubek, D. Hypoxanthine as a graft ischemia marker stimulates catalase activity in the renal vein during reperfusion in humans, Transplantation Proceedings. 38, 35–38. – volume: 308 start-page: 1909 year: 2005 end-page: 1911 ident: bib102 article-title: Extension of murine life span by overexpression of catalase targeted to mitochondria publication-title: Science – volume: 96 start-page: 307 year: 2016 end-page: 364 ident: bib63 article-title: Paradoxical roles of antioxidant enzymes: basic mechanisms and health implications publication-title: Physiol. Rev. – volume: 72 start-page: 19 year: 1999 end-page: 66 ident: bib137 article-title: Understanding the structure and function of catalases: clues from molecular evolution and in vitro mutagenesis publication-title: Prog. Biophys. Mol. Biol. – volume: 1777 start-page: 1032 year: 2008 end-page: 1037 ident: bib79 article-title: Distance metrics for heme protein electron tunneling publication-title: Biochim. Biophys. Acta – volume: 35 start-page: 69 year: 2002 end-page: 72 ident: bib86 article-title: Lens superoxide dismutase and catalase activities in diabetic cataract publication-title: Clin. Biochem. – volume: 39 start-page: 610 year: 1960 end-page: 619 ident: bib115 article-title: Hypocatalasemia: a new genetic Carrier state publication-title: J. Clin. Invest. – volume: 171 start-page: 10 year: 2017 end-page: 17 ident: bib57 article-title: Interactions of nitrite with catalase: enzyme activity and reaction kinetics studies publication-title: J. Inorg. Biochem. – volume: 630 start-page: 81 year: 2017 end-page: 90 ident: bib72 article-title: Destructive effect of non-enzymatic glycation on catalase and remediation via curcumin publication-title: Arch. Biochem. Biophys. – volume: 11 start-page: 26 year: 1989 end-page: 28 ident: bib76 article-title: Thermodynamics of the interaction of sodium-n-dodecyl sulphate with Aspergillus Niger catalase in high ionic strength aqueous solutions publication-title: Int. J. Biol. Macromol. – volume: 913 start-page: 395 year: 1987 end-page: 398 ident: bib47 article-title: The activation of Aspergillus Niger catalase by sodium n-dodecyl-sulphate publication-title: Biochim. Biophys. Acta – volume: 118 start-page: 2924 year: 2014 end-page: 2931 ident: bib124 article-title: Binding of the antitubercular pro-drug isoniazid in the heme access channel of catalase-peroxidase (KatG). A combined structural and metadynamics investigation publication-title: J. Phys. Chem. B – year: 2000 ident: bib114 article-title: Heme-fe Proteins – volume: 279 start-page: 32804 year: 2004 end-page: 32812 ident: bib38 article-title: Mice lacking catalase develop normally but show differential sensitivity to oxidant tissue injury publication-title: J. Biol. Chem. – volume: 104 start-page: 648 year: 2010 end-page: 656 ident: bib126 article-title: Disruption of the H-bond network in the main access channel of catalase-peroxidase modulates enthalpy and entropy of Fe(III) reduction publication-title: J. Inorg. Biochem. – volume: 14 start-page: 201 year: 1972 end-page: 205 ident: bib83 article-title: Inactivation of immobilized catalase by hydrogen peroxide in continuous reactors publication-title: Biotechnol. Bioeng. – volume: 24 start-page: 1 year: 2004 end-page: 52 ident: bib87 article-title: Thermodynamics of protein–ligand interactions: history, presence, and future aspects publication-title: J. Recept. Signal Transduct. Res. – volume: 6 start-page: 1395 year: 1987 end-page: 1402 ident: bib17 article-title: Hydrogen peroxide in the rabbit anterior chamber: effects on glutathione, and catalase effects on peroxide kinetics publication-title: Curr. Eye Res. – volume: 293 start-page: 411 year: 1981 end-page: 412 ident: bib121 article-title: Three-dimensional structure of the enzyme catalase publication-title: Nature – volume: 279 start-page: 43098 year: 2004 end-page: 43106 ident: bib107 article-title: Catalase-peroxidases (KatG) exhibit NADH oxidase activity publication-title: J. Biol. Chem. – year: 2010 ident: bib21 article-title: Peroxidases and Catalases: Biochemistry, Biophysics, Biotechnology and Physiology – volume: 189 start-page: 201 year: 1991 end-page: 207 ident: bib73 article-title: Thermochemical analysis of Aspergillus Niger catalase and sodium n-dodecyl sulphate interaction publication-title: Thermochim. Acta – volume: 280 start-page: 9037 year: 2005 end-page: 9042 ident: bib44 article-title: Kinetics of interconversion of ferrous enzymes, compound II and compound III, of wild-type synechocystis catalase-peroxidase and Y249F: proposal for the catalatic mechanism publication-title: J. Biol. Chem. – volume: 20 start-page: 131 year: 2005 end-page: 135 ident: bib14 article-title: Catalase: a repertoire of unusual features publication-title: Indian J. Clin. Biochem. – volume: 11 start-page: 701 year: 1900 end-page: 702 ident: bib65 article-title: A new enzyme of general occurrence in organisms publication-title: Science – volume: 85 start-page: 366 year: 1937 end-page: 367 ident: bib112 article-title: Crystalline catalase publication-title: Science – volume: 9 start-page: 327 year: 1987 end-page: 332 ident: bib75 article-title: Characterization of Aspergillus Niger catalase publication-title: Int. J. Biol. Macromol. – volume: 21 start-page: 257 year: 2016 end-page: 263 ident: bib138 article-title: Protective effect of an isoflavone, tectorigenin, against oxidative stress-induced cell death via catalase activation publication-title: J. Cancer Prev. – volume: 252 start-page: 1 year: 2007 end-page: 8 ident: bib66 article-title: Dual role of hydrogen peroxide in cancer: possible relevance to cancer chemoprevention and therapy publication-title: Canc. Lett. – volume: 19 start-page: 1292 year: 2003 end-page: 1299 ident: bib118 article-title: Purification and characterization of a novel thermo-alkali-stable catalase from Thermus brockianus publication-title: Biotechnol. Prog. – volume: 4 year: 2012 ident: bib34 article-title: Avogadro: an advanced semantic chemical editor, visualization, and analysis platform publication-title: J. Cheminf. – volume: 7 start-page: 619 year: 2005 end-page: 626 ident: bib94 article-title: Controlled elimination of intracellular H(2)O(2): regulation of peroxiredoxin, catalase, and glutathione peroxidase via post-translational modification publication-title: Antioxidants Redox Signal. – volume: 94 start-page: e679 year: 2015 ident: bib104 article-title: The catalase C-262T gene polymorphism and cancer risk: a systematic review and meta-analysis publication-title: Medicine (Baltim.) – volume: 9 start-page: 555 year: 2002 end-page: 565 ident: bib122 article-title: Suicide inactivation of peroxidases and the challenge of engineering more robust enzymes publication-title: Chem. Biol. – volume: 128 start-page: 35 year: 2013 end-page: 42 ident: bib130 article-title: Binding of chrysoidine to catalase: spectroscopy, isothermal titration calorimetry and molecular docking studies publication-title: J. Photochem. Photobiol., B – volume: 11 start-page: 1285 year: 2002 end-page: 1299 ident: bib64 article-title: 3D domain swapping: as domains continue to swap publication-title: Protein Sci. : Publ. Protein Soc. – volume: 320 start-page: 61 year: 1996 end-page: 67 ident: bib42 article-title: Importance of catalase in the adaptive response to hydrogen peroxide: analysis of acatalasaemic Saccharomyces cerevisiae publication-title: Biochem. J. – year: 2007 ident: bib5 article-title: Redox Biochemistry – volume: 135 start-page: 15579 year: 2013 end-page: 15584 ident: bib9 article-title: Water networks contribute to enthalpy/entropy compensation in protein–ligand binding publication-title: J. Am. Chem. Soc. – volume: 80 start-page: 379 year: 2007 end-page: 393 ident: bib125 article-title: Measurements of the antioxidant enzyme activities of superoxide dismutase, catalase, and glutathione peroxidase publication-title: Meth. Cell Biol. – volume: 356 start-page: 1820 year: 2000 end-page: 1821 ident: bib31 article-title: Hereditary catalase deficiencies and increased risk of diabetes publication-title: Lancet – volume: 262 start-page: 9608 year: 1987 end-page: 9614 ident: bib90 article-title: Ethanenitronate is a peroxide-dependent suicide substrate for catalase publication-title: J. Biol. Chem. – volume: 184 start-page: 139 year: 1990 end-page: 144 ident: bib23 article-title: On the application of the Clark oxygen electrode to the study of enzyme kinetics in apolar solvents: the catalase reaction publication-title: Anal. Biochem. – volume: 753 start-page: 147 year: 2013 end-page: 154 ident: bib32 article-title: Inherited catalase deficiency: is it benign or a factor in various age related disorders? publication-title: Mutat. Res. Rev. Mutat. Res. – volume: 86 start-page: 308 year: 2015 end-page: 321 ident: bib119 article-title: A comprehensive evaluation of catalase-like activity of different classes of redox-active therapeutics publication-title: Free Radic. Biol. Med. – volume: 152 start-page: 465 year: 1981 end-page: 499 ident: bib81 article-title: Structure of beef liver catalase publication-title: J. Mol. Biol. – volume: 279 start-page: 98 year: 1998 end-page: 102 ident: bib98 article-title: Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis publication-title: Science – volume: 58 start-page: 148 year: 2013 end-page: 153 ident: bib58 article-title: Catalase is inhibited by flavonoids publication-title: Int. J. Biol. Macromol. – volume: 252 start-page: 3582 year: 1977 end-page: 3586 ident: bib1 article-title: Effect of covalent attachment of polyethylene glycol on immunogenicity and circulating life of bovine liver catalase publication-title: J. Biol. Chem. – volume: 7 start-page: 46696 year: 2017 ident: bib68 article-title: Functional, thermodynamics, structural and biological studies of in silico-identified inhibitors of Mycobacterium tuberculosis enoyl-ACP(CoA) reductase enzyme publication-title: Sci. Rep. – volume: 82 start-page: 1604 year: 1985 end-page: 1608 ident: bib24 article-title: The NADPH binding site on beef liver catalase publication-title: Proc. Natl. Acad. Sci. U.S.A. – volume: 87 start-page: 284 year: 1938 ident: bib113 article-title: The molecular weight of crystalline catalase publication-title: Science – year: 2016, Garland Science ident: bib16 article-title: Biochemical Evolution: The Pursuit of Perfection – volume: 44 start-page: D1202 year: 2016 end-page: D1213 ident: bib50 article-title: PubChem substance and compound databases publication-title: Nucleic Acids Res. – volume: 8 start-page: 243 year: 2006 end-page: 270 ident: bib110 article-title: Hydrogen peroxide: a signaling messenger publication-title: Antioxidants Redox Signal. – volume: 41 start-page: 1574 year: 1995 end-page: 1580 ident: bib133 article-title: Serum catalase as marker of graft-vs-host disease in allogeneic bone marrow transplant recipients: pilot study publication-title: Clin. Chem. – volume: 717 start-page: 60 year: 1994 end-page: 71 ident: bib52 article-title: (-)Deprenyl increases the life span as well as activities of superoxide dismutase and catalase but not of glutathione peroxidase in selective brain regions in Fischer rats publication-title: Ann. N. Y. Acad. Sci. – volume: 48 start-page: 1334 year: 2014 end-page: 1341 ident: bib59 article-title: Flavonoid-induced conversion of catalase to its inactive form–Compound II publication-title: Free Radic. Res. – volume: 30 start-page: 2648 year: 2017 end-page: 2658 ident: bib134 article-title: Activation of catalase by pioglitazone: multiple spectroscopic methods combined with molecular docking studies publication-title: J. Mol. Recogn. – volume: 133 start-page: 51 year: 1983 end-page: 69 ident: bib22 article-title: The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution publication-title: Eur. J. Biochem. – volume: 13 start-page: 869 year: 2008 end-page: 874 ident: bib25 article-title: Do enthalpy and entropy distinguish first in class from best in class? publication-title: Drug Discov. Today – volume: 8 start-page: 316 year: 2007 ident: bib89 article-title: Versatile annotation and publication quality visualization of protein complexes using POLYVIEW-3D publication-title: BMC Bioinf. – volume: 383 start-page: 841 year: 2014 end-page: 843 ident: bib128 article-title: Type 2 diabetes as a redox disease publication-title: Lancet – volume: 29 start-page: 99 year: 2001 end-page: 105 ident: bib92 article-title: The role of distal tryptophan in the bifunctional activity of catalase-peroxidases publication-title: Biochem. Soc. Trans. – volume: 51 start-page: 163 year: 1948 end-page: 168 ident: bib116 article-title: Three cases of progressive oral gangrene due to lack of catalase in the blood publication-title: Jpn. J. Otol. – volume: 28 start-page: 209 year: 2006 end-page: 218 ident: bib101 article-title: Extension of mouse lifespan by overexpression of catalase publication-title: Age – volume: 73 start-page: 2043 year: 1976 end-page: 2046 ident: bib62 article-title: A fatty acyl-CoA oxidizing system in rat liver peroxisomes; enhancement by clofibrate, a hypolipidemic drug publication-title: Proc. Natl. Acad. Sci. Unit. States Am. – volume: 80 start-page: 409 year: 1977 end-page: 415 ident: bib19 article-title: A more sensitive modification of the catalase assay with the Clark oxygen electrode. Application to the kinetic study of the pea leaf enzyme publication-title: Anal. Biochem. – volume: 49 start-page: 173 year: 1994 end-page: 189 ident: bib123 article-title: Soluble and immobilized catalase. Effect of pressure and inhibition on kinetics and deactivation publication-title: Appl. Biochem. Biotechnol. – volume: 17 start-page: 235 year: 1994 end-page: 248 ident: bib70 article-title: Importance of Se-glutathione peroxidase, catalase, and Cu/Zn-SOD for cell survival against oxidative stress publication-title: Free Radic. Biol. Med. – volume: 100 start-page: 568 year: 2006 end-page: 585 ident: bib108 article-title: Probing the structure and bifunctionality of catalase-peroxidase (KatG) publication-title: J. Inorg. Biochem. – volume: 95 start-page: 1075 year: 2004 end-page: 1081 ident: bib131 article-title: Retardation of atherosclerosis by overexpression of catalase or both Cu/Zn-superoxide dismutase and catalase in mice lacking apolipoprotein E publication-title: Circ. Res. – volume: 10 start-page: 75 year: 1988 end-page: 78 ident: bib74 article-title: Thermodynamics of the interaction of sodium n-dodecyl sulphate with Aspergillus Niger catalase in low ionic strength aqueous solutions publication-title: Int. J. Biol. Macromol. – volume: 258 start-page: 10558 year: 1983 end-page: 10563 ident: bib85 article-title: Inactivation of catalase by phenylhydrazine. Formation of a stable aryl-iron heme complex publication-title: J. Biol. Chem. – volume: 489 start-page: 124 year: 2015 end-page: 130 ident: bib99 article-title: Arrhenius activation energy of damage to catalase during spray-drying publication-title: Int. J. Pharm. – volume: 19 start-page: 1096 year: 1995 end-page: 1104 ident: bib55 article-title: Family history of alcoholism and the mediation of alcohol intake by catalase: further evidence for catalase as a marker of the propensity to ingest alcohol publication-title: Alcohol Clin. Exp. Res. – volume: 284 start-page: 7017 year: 2009 end-page: 7029 ident: bib111 article-title: An oxyferrous heme/protein-based radical intermediate is catalytically competent in the catalase reaction of mycobacterium tuberculosis catalase-peroxidase (KatG) publication-title: J. Biol. Chem. – volume: 27 start-page: 141 year: 2008 end-page: 145 ident: bib48 article-title: The interrelation of glutathione reductase, catalase, glutathione peroxidase, superoxide dismutase, and glucose-6-phosphate in the pathogenesis of rheumatoid arthritis publication-title: Clin. Rheumatol. – volume: 98 start-page: 235 year: 1975 ident: 10.1016/j.pbiomolbio.2018.03.001_bib120 article-title: Beef liver catalase structure: interpretation of electron micrographs publication-title: J. Mol. Biol. doi: 10.1016/S0022-2836(75)80111-2 – volume: 80 start-page: 379 year: 2007 ident: 10.1016/j.pbiomolbio.2018.03.001_bib125 article-title: Measurements of the antioxidant enzyme activities of superoxide dismutase, catalase, and glutathione peroxidase publication-title: Meth. Cell Biol. doi: 10.1016/S0091-679X(06)80019-1 – volume: 293 start-page: 411 year: 1981 ident: 10.1016/j.pbiomolbio.2018.03.001_bib121 article-title: Three-dimensional structure of the enzyme catalase publication-title: Nature doi: 10.1038/293411a0 – volume: 71 start-page: 4681 year: 2014 ident: 10.1016/j.pbiomolbio.2018.03.001_bib135 article-title: Turning points in the evolution of peroxidase-catalase superfamily: molecular phylogeny of hybrid heme peroxidases publication-title: Cell. Mol. Life Sci. doi: 10.1007/s00018-014-1643-y – year: 2010 ident: 10.1016/j.pbiomolbio.2018.03.001_bib21 – volume: 31 start-page: 1440 year: 2013 ident: 10.1016/j.pbiomolbio.2018.03.001_bib103 article-title: Effect of compatible and noncompatible osmolytes on the enzymatic activity and thermal stability of bovine liver catalase publication-title: J. Biomol. Struct. Dyn. doi: 10.1080/07391102.2012.742460 – volume: 100 start-page: 568 year: 2006 ident: 10.1016/j.pbiomolbio.2018.03.001_bib108 article-title: Probing the structure and bifunctionality of catalase-peroxidase (KatG) publication-title: J. Inorg. Biochem. doi: 10.1016/j.jinorgbio.2006.01.033 – volume: 308 start-page: 1909 year: 2005 ident: 10.1016/j.pbiomolbio.2018.03.001_bib102 article-title: Extension of murine life span by overexpression of catalase targeted to mitochondria publication-title: Science doi: 10.1126/science.1106653 – volume: 10 start-page: 167 year: 1996 ident: 10.1016/j.pbiomolbio.2018.03.001_bib27 article-title: Determination of the kinetic parameters for the “suicide substrate” inactivation of bovine liver catalase by hydrogen peroxide publication-title: J. Enzym. Inhib. doi: 10.3109/14756369609030310 – year: 2004 ident: 10.1016/j.pbiomolbio.2018.03.001_bib39 – volume: 258 start-page: 10558 year: 1983 ident: 10.1016/j.pbiomolbio.2018.03.001_bib85 article-title: Inactivation of catalase by phenylhydrazine. Formation of a stable aryl-iron heme complex publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)44492-9 – volume: 48 start-page: 9 year: 1999 ident: 10.1016/j.pbiomolbio.2018.03.001_bib77 article-title: Suicide inactivation of peroxidase by H2O2: kinetic equations for peroxidatic oxidation reaction of guaiacol and determination of the kinetic parameters publication-title: Ital. J. Biochem. – volume: 218 start-page: 243 year: 1968 ident: 10.1016/j.pbiomolbio.2018.03.001_bib11 article-title: Semipermeable microcapsules containing catalase for enzyme replacement in acatalasaemic mice publication-title: Nature doi: 10.1038/218243a0 – volume: 128 start-page: 113 year: 2017 ident: 10.1016/j.pbiomolbio.2018.03.001_bib69 article-title: Understanding protein domain-swapping using structure-based models of protein folding publication-title: Prog. Biophys. Mol. Biol. doi: 10.1016/j.pbiomolbio.2016.09.013 – volume: 84 start-page: 325 year: 1994 ident: 10.1016/j.pbiomolbio.2018.03.001_bib26 article-title: Importance of catalase in the disposal of hydrogen peroxide within human erythrocytes publication-title: Blood doi: 10.1182/blood.V84.1.325.325 – volume: 152 start-page: 465 year: 1981 ident: 10.1016/j.pbiomolbio.2018.03.001_bib81 article-title: Structure of beef liver catalase publication-title: J. Mol. Biol. doi: 10.1016/0022-2836(81)90254-0 – volume: 280 start-page: 42411 year: 2005 ident: 10.1016/j.pbiomolbio.2018.03.001_bib43 article-title: Role of the main access channel of catalase-peroxidase in catalysis publication-title: J. Biol. Chem. doi: 10.1074/jbc.M508009200 – start-page: 1 year: 2017 ident: 10.1016/j.pbiomolbio.2018.03.001_bib49 article-title: Cationic surfactant mediated fibrillogenesis in bovine liver catalase: a biophysical approach publication-title: J. Biomol. Struct. Dyn. – volume: 49 start-page: 173 year: 1994 ident: 10.1016/j.pbiomolbio.2018.03.001_bib123 article-title: Soluble and immobilized catalase. Effect of pressure and inhibition on kinetics and deactivation publication-title: Appl. Biochem. Biotechnol. doi: 10.1007/BF02783056 – volume: 753 start-page: 147 year: 2013 ident: 10.1016/j.pbiomolbio.2018.03.001_bib32 article-title: Inherited catalase deficiency: is it benign or a factor in various age related disorders? publication-title: Mutat. Res. Rev. Mutat. Res. doi: 10.1016/j.mrrev.2013.08.002 – volume: 10 start-page: 75 year: 1988 ident: 10.1016/j.pbiomolbio.2018.03.001_bib74 article-title: Thermodynamics of the interaction of sodium n-dodecyl sulphate with Aspergillus Niger catalase in low ionic strength aqueous solutions publication-title: Int. J. Biol. Macromol. doi: 10.1016/0141-8130(88)90014-1 – volume: 72 start-page: 19 year: 1999 ident: 10.1016/j.pbiomolbio.2018.03.001_bib137 article-title: Understanding the structure and function of catalases: clues from molecular evolution and in vitro mutagenesis publication-title: Prog. Biophys. Mol. Biol. doi: 10.1016/S0079-6107(98)00058-3 – volume: 20 start-page: 131 year: 2005 ident: 10.1016/j.pbiomolbio.2018.03.001_bib14 article-title: Catalase: a repertoire of unusual features publication-title: Indian J. Clin. Biochem. doi: 10.1007/BF02867412 – volume: 104 start-page: 648 year: 2010 ident: 10.1016/j.pbiomolbio.2018.03.001_bib126 article-title: Disruption of the H-bond network in the main access channel of catalase-peroxidase modulates enthalpy and entropy of Fe(III) reduction publication-title: J. Inorg. Biochem. doi: 10.1016/j.jinorgbio.2010.02.006 – volume: 118 start-page: 2924 year: 2014 ident: 10.1016/j.pbiomolbio.2018.03.001_bib124 article-title: Binding of the antitubercular pro-drug isoniazid in the heme access channel of catalase-peroxidase (KatG). A combined structural and metadynamics investigation publication-title: J. Phys. Chem. B doi: 10.1021/jp4123425 – volume: 252 start-page: 3582 year: 1977 ident: 10.1016/j.pbiomolbio.2018.03.001_bib1 article-title: Effect of covalent attachment of polyethylene glycol on immunogenicity and circulating life of bovine liver catalase publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)40292-4 – volume: 356 start-page: 1820 year: 2000 ident: 10.1016/j.pbiomolbio.2018.03.001_bib31 article-title: Hereditary catalase deficiencies and increased risk of diabetes publication-title: Lancet doi: 10.1016/S0140-6736(00)03238-4 – volume: 30 start-page: 2648 year: 2017 ident: 10.1016/j.pbiomolbio.2018.03.001_bib134 article-title: Activation of catalase by pioglitazone: multiple spectroscopic methods combined with molecular docking studies publication-title: J. Mol. Recogn. doi: 10.1002/jmr.2648 – volume: 11 start-page: 701 year: 1900 ident: 10.1016/j.pbiomolbio.2018.03.001_bib65 article-title: A new enzyme of general occurrence in organisms publication-title: Science doi: 10.1126/science.11.279.701 – volume: 280 start-page: 9037 year: 2005 ident: 10.1016/j.pbiomolbio.2018.03.001_bib44 article-title: Kinetics of interconversion of ferrous enzymes, compound II and compound III, of wild-type synechocystis catalase-peroxidase and Y249F: proposal for the catalatic mechanism publication-title: J. Biol. Chem. doi: 10.1074/jbc.M413317200 – volume: 87 start-page: 284 year: 1938 ident: 10.1016/j.pbiomolbio.2018.03.001_bib113 article-title: The molecular weight of crystalline catalase publication-title: Science doi: 10.1126/science.87.2256.284 – volume: 1431 start-page: 30 year: 1999 ident: 10.1016/j.pbiomolbio.2018.03.001_bib28 article-title: Influence of different types of effectors on the kinetic parameters of suicide inactivation of catalase by hydrogen peroxide publication-title: Biochim. Biophys. Acta doi: 10.1016/S0167-4838(99)00021-7 – volume: 41 start-page: 953 year: 2007 ident: 10.1016/j.pbiomolbio.2018.03.001_bib30 article-title: Catalase deficiency may complicate urate oxidase (rasburicase) therapy publication-title: Free Radic. Res. doi: 10.1080/10715760701482451 – volume: 279 start-page: 43098 year: 2004 ident: 10.1016/j.pbiomolbio.2018.03.001_bib107 article-title: Catalase-peroxidases (KatG) exhibit NADH oxidase activity publication-title: J. Biol. Chem. doi: 10.1074/jbc.M406374200 – volume: 94 start-page: e679 year: 2015 ident: 10.1016/j.pbiomolbio.2018.03.001_bib104 article-title: The catalase C-262T gene polymorphism and cancer risk: a systematic review and meta-analysis publication-title: Medicine (Baltim.) doi: 10.1097/MD.0000000000000679 – volume: 284 start-page: 7017 year: 2009 ident: 10.1016/j.pbiomolbio.2018.03.001_bib111 article-title: An oxyferrous heme/protein-based radical intermediate is catalytically competent in the catalase reaction of mycobacterium tuberculosis catalase-peroxidase (KatG) publication-title: J. Biol. Chem. doi: 10.1074/jbc.M808106200 – volume: 146 start-page: 215 year: 1989 ident: 10.1016/j.pbiomolbio.2018.03.001_bib78 article-title: Thermodynamics of the interaction between n-dodecyltrimethylammonium bromide and catalases publication-title: Thermochim. Acta doi: 10.1016/0040-6031(89)87090-X – year: 2013 ident: 10.1016/j.pbiomolbio.2018.03.001_bib15 – volume: 66 start-page: 654 year: 2010 ident: 10.1016/j.pbiomolbio.2018.03.001_bib4 article-title: Flexibility of the Cu,Zn superoxide dismutase structure investigated at 0.57 GPa publication-title: Acta Crystallogr. Sect. D Biol. Crystallogr. doi: 10.1107/S0907444910012321 – volume: 35 start-page: 69 year: 2002 ident: 10.1016/j.pbiomolbio.2018.03.001_bib86 article-title: Lens superoxide dismutase and catalase activities in diabetic cataract publication-title: Clin. Biochem. doi: 10.1016/S0009-9120(01)00284-3 – volume: 113 start-page: 591 year: 2013 ident: 10.1016/j.pbiomolbio.2018.03.001_bib117 article-title: Correlation between biological activity and electron transferring of bovine liver catalase: osmolytes effects publication-title: Electrochim. Acta doi: 10.1016/j.electacta.2013.09.100 – volume: 128 start-page: 35 year: 2013 ident: 10.1016/j.pbiomolbio.2018.03.001_bib130 article-title: Binding of chrysoidine to catalase: spectroscopy, isothermal titration calorimetry and molecular docking studies publication-title: J. Photochem. Photobiol., B doi: 10.1016/j.jphotobiol.2013.08.006 – volume: 94 start-page: 615 year: 1941 ident: 10.1016/j.pbiomolbio.2018.03.001_bib61 article-title: Crystalline catalase from beef erythrocytes publication-title: Science doi: 10.1126/science.94.2452.615 – volume: 32 start-page: 44 year: 2007 ident: 10.1016/j.pbiomolbio.2018.03.001_bib51 article-title: Mammalian catalase: a venerable enzyme with new mysteries publication-title: Trends Biochem. Sci. doi: 10.1016/j.tibs.2006.11.003 – volume: 39 start-page: 610 year: 1960 ident: 10.1016/j.pbiomolbio.2018.03.001_bib115 article-title: Hypocatalasemia: a new genetic Carrier state publication-title: J. Clin. Invest. doi: 10.1172/JCI104075 – volume: 383 start-page: 841 year: 2014 ident: 10.1016/j.pbiomolbio.2018.03.001_bib128 article-title: Type 2 diabetes as a redox disease publication-title: Lancet doi: 10.1016/S0140-6736(13)62365-X – volume: 102 start-page: 88 year: 2013 ident: 10.1016/j.pbiomolbio.2018.03.001_bib127 article-title: Spectroscopic study on the interaction of catalase with bifendate and analogs publication-title: Spectrochim. Acta Mol. Biomol. Spectrosc. doi: 10.1016/j.saa.2012.10.039 – volume: 99 start-page: 4097 year: 2002 ident: 10.1016/j.pbiomolbio.2018.03.001_bib132 article-title: Hydrogen peroxide homeostasis: activation of plant catalase by calcium/calmodulin publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.052564899 – volume: 195 start-page: 133 year: 1952 ident: 10.1016/j.pbiomolbio.2018.03.001_bib6 article-title: A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)50881-X – volume: 28 start-page: 711 year: 2012 ident: 10.1016/j.pbiomolbio.2018.03.001_bib40 article-title: A highly efficient nano-cluster artificial peroxidase and its direct electrochemistry on a nano complex modified glassy carbon electrode publication-title: Anal. Sci. doi: 10.2116/analsci.28.711 – year: 2011 ident: 10.1016/j.pbiomolbio.2018.03.001_bib12 – volume: 7 start-page: 619 year: 2005 ident: 10.1016/j.pbiomolbio.2018.03.001_bib94 article-title: Controlled elimination of intracellular H(2)O(2): regulation of peroxiredoxin, catalase, and glutathione peroxidase via post-translational modification publication-title: Antioxidants Redox Signal. doi: 10.1089/ars.2005.7.619 – volume: 717 start-page: 60 year: 1994 ident: 10.1016/j.pbiomolbio.2018.03.001_bib52 article-title: (-)Deprenyl increases the life span as well as activities of superoxide dismutase and catalase but not of glutathione peroxidase in selective brain regions in Fischer rats publication-title: Ann. N. Y. Acad. Sci. doi: 10.1111/j.1749-6632.1994.tb12073.x – volume: 8 start-page: 316 year: 2007 ident: 10.1016/j.pbiomolbio.2018.03.001_bib89 article-title: Versatile annotation and publication quality visualization of protein complexes using POLYVIEW-3D publication-title: BMC Bioinf. doi: 10.1186/1471-2105-8-316 – volume: 913 start-page: 395 year: 1987 ident: 10.1016/j.pbiomolbio.2018.03.001_bib47 article-title: The activation of Aspergillus Niger catalase by sodium n-dodecyl-sulphate publication-title: Biochim. Biophys. Acta doi: 10.1016/0167-4838(87)90151-8 – volume: 9 start-page: 23 year: 2010 ident: 10.1016/j.pbiomolbio.2018.03.001_bib60 article-title: Adding calorimetric data to decision making in lead discovery: a hot tip publication-title: Nat. Rev. Drug Discov. doi: 10.1038/nrd3054 – volume: 86 start-page: 308 year: 2015 ident: 10.1016/j.pbiomolbio.2018.03.001_bib119 article-title: A comprehensive evaluation of catalase-like activity of different classes of redox-active therapeutics publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2015.05.018 – volume: 278 start-page: 22432 year: 2003 ident: 10.1016/j.pbiomolbio.2018.03.001_bib36 article-title: UVB light stimulates production of reactive oxygen species: unexpected role for catalase publication-title: J. Biol. Chem. doi: 10.1074/jbc.C300048200 – volume: 96 start-page: 307 year: 2016 ident: 10.1016/j.pbiomolbio.2018.03.001_bib63 article-title: Paradoxical roles of antioxidant enzymes: basic mechanisms and health implications publication-title: Physiol. Rev. doi: 10.1152/physrev.00010.2014 – volume: 1252 start-page: 172 year: 1995 ident: 10.1016/j.pbiomolbio.2018.03.001_bib7 article-title: Simulations of electron transfer in the NADPH-bound catalase from Proteus mirabilis PR publication-title: Biochim. Biophys. Acta doi: 10.1016/0167-4838(95)00123-C – volume: 44 start-page: D1202 year: 2016 ident: 10.1016/j.pbiomolbio.2018.03.001_bib50 article-title: PubChem substance and compound databases publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkv951 – volume: 9 start-page: 555 year: 2002 ident: 10.1016/j.pbiomolbio.2018.03.001_bib122 article-title: Suicide inactivation of peroxidases and the challenge of engineering more robust enzymes publication-title: Chem. Biol. doi: 10.1016/S1074-5521(02)00149-7 – volume: 28 start-page: 209 year: 2006 ident: 10.1016/j.pbiomolbio.2018.03.001_bib101 article-title: Extension of mouse lifespan by overexpression of catalase publication-title: Age doi: 10.1007/s11357-006-9010-z – year: 2000 ident: 10.1016/j.pbiomolbio.2018.03.001_bib114 – volume: 320 start-page: 61 issue: Pt 1 year: 1996 ident: 10.1016/j.pbiomolbio.2018.03.001_bib42 article-title: Importance of catalase in the adaptive response to hydrogen peroxide: analysis of acatalasaemic Saccharomyces cerevisiae publication-title: Biochem. J. doi: 10.1042/bj3200061 – volume: 262 start-page: 9608 year: 1987 ident: 10.1016/j.pbiomolbio.2018.03.001_bib90 article-title: Ethanenitronate is a peroxide-dependent suicide substrate for catalase publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)47977-X – volume: 48 start-page: 447 year: 1996 ident: 10.1016/j.pbiomolbio.2018.03.001_bib53 publication-title: Exp. Toxicol. Pathol. doi: 10.1016/S0940-2993(96)80055-8 – volume: 34 start-page: 81 year: 2007 ident: 10.1016/j.pbiomolbio.2018.03.001_bib129 article-title: Cardiac-specific overexpression of catalase prolongs lifespan and attenuates ageing-induced cardiomyocyte contractile dysfunction and protein damage publication-title: Clin. Exp. Pharmacol. Physiol. doi: 10.1111/j.1440-1681.2007.04540.x – volume: 95 start-page: 1075 year: 2004 ident: 10.1016/j.pbiomolbio.2018.03.001_bib131 article-title: Retardation of atherosclerosis by overexpression of catalase or both Cu/Zn-superoxide dismutase and catalase in mice lacking apolipoprotein E publication-title: Circ. Res. doi: 10.1161/01.RES.0000149564.49410.0d – volume: 367 start-page: 241 year: 1995 ident: 10.1016/j.pbiomolbio.2018.03.001_bib136 article-title: Site-directed mutagenesis of the lower parts of the major substrate channel of yeast catalase A leads to highly increased peroxidatic activity publication-title: FEBS Lett. doi: 10.1016/0014-5793(95)00568-T – volume: 33 start-page: 401 year: 1984 ident: 10.1016/j.pbiomolbio.2018.03.001_bib80 article-title: Visualization of surface structure of catalase crystals by metal decoration publication-title: J. Electron. Microsc.(Tokyo) – volume: 29 start-page: 99 year: 2001 ident: 10.1016/j.pbiomolbio.2018.03.001_bib92 article-title: The role of distal tryptophan in the bifunctional activity of catalase-peroxidases publication-title: Biochem. Soc. Trans. doi: 10.1042/bst0290099 – year: 2007 ident: 10.1016/j.pbiomolbio.2018.03.001_bib3 – volume: 7 start-page: 46696 year: 2017 ident: 10.1016/j.pbiomolbio.2018.03.001_bib68 article-title: Functional, thermodynamics, structural and biological studies of in silico-identified inhibitors of Mycobacterium tuberculosis enoyl-ACP(CoA) reductase enzyme publication-title: Sci. Rep. doi: 10.1038/srep46696 – volume: 630 start-page: 81 year: 2017 ident: 10.1016/j.pbiomolbio.2018.03.001_bib72 article-title: Destructive effect of non-enzymatic glycation on catalase and remediation via curcumin publication-title: Arch. Biochem. Biophys. doi: 10.1016/j.abb.2017.06.018 – year: 2007 ident: 10.1016/j.pbiomolbio.2018.03.001_bib37 – volume: 105 start-page: 121 year: 1984 ident: 10.1016/j.pbiomolbio.2018.03.001_bib2 article-title: Catalase in vitro publication-title: Methods Enzymol. doi: 10.1016/S0076-6879(84)05016-3 – volume: 139 start-page: 171 year: 1967 ident: 10.1016/j.pbiomolbio.2018.03.001_bib95 article-title: Determination of catalase activity by means of the Clark oxygen electrode publication-title: Biochim. Biophys. Acta doi: 10.1016/0005-2744(67)90124-6 – volume: 73 start-page: 2043 year: 1976 ident: 10.1016/j.pbiomolbio.2018.03.001_bib62 article-title: A fatty acyl-CoA oxidizing system in rat liver peroxisomes; enhancement by clofibrate, a hypolipidemic drug publication-title: Proc. Natl. Acad. Sci. Unit. States Am. doi: 10.1073/pnas.73.6.2043 – volume: 51 start-page: 51 year: 2000 ident: 10.1016/j.pbiomolbio.2018.03.001_bib82 article-title: Enzymology and structure of catalases publication-title: Adv. Inorg. Chem. doi: 10.1016/S0898-8838(00)51001-0 – volume: 55 start-page: 1383 year: 1999 ident: 10.1016/j.pbiomolbio.2018.03.001_bib54 article-title: Structure of orthorhombic crystals of beef liver catalase publication-title: Acta Crystallogr. Sect. D Biol. Crystallogr. doi: 10.1107/S0907444999007052 – volume: 104 start-page: 2121 year: 2007 ident: 10.1016/j.pbiomolbio.2018.03.001_bib18 article-title: Reactive oxygen species detoxification by catalase is a major determinant of fecundity in the mosquito Anopheles gambiae publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.0608407104 – volume: 17 start-page: 235 year: 1994 ident: 10.1016/j.pbiomolbio.2018.03.001_bib70 article-title: Importance of Se-glutathione peroxidase, catalase, and Cu/Zn-SOD for cell survival against oxidative stress publication-title: Free Radic. Biol. Med. doi: 10.1016/0891-5849(94)90079-5 – volume: 300 start-page: 258 year: 1993 ident: 10.1016/j.pbiomolbio.2018.03.001_bib88 article-title: tBOOH acts as a suicide substrate for catalase publication-title: Arch. Biochem. Biophys. doi: 10.1006/abbi.1993.1036 – volume: 14 start-page: 201 year: 1972 ident: 10.1016/j.pbiomolbio.2018.03.001_bib83 article-title: Inactivation of immobilized catalase by hydrogen peroxide in continuous reactors publication-title: Biotechnol. Bioeng. doi: 10.1002/bit.260140205 – volume: 11 start-page: 1285 year: 2002 ident: 10.1016/j.pbiomolbio.2018.03.001_bib64 article-title: 3D domain swapping: as domains continue to swap publication-title: Protein Sci. : Publ. Protein Soc. doi: 10.1110/ps.0201402 – volume: 56 start-page: 2271 year: 2017 ident: 10.1016/j.pbiomolbio.2018.03.001_bib67 article-title: The catalase activity of catalase-peroxidases is modulated by changes in the pKa of the distal histidine publication-title: Biochemistry doi: 10.1021/acs.biochem.6b01276 – volume: 9 start-page: 327 year: 1987 ident: 10.1016/j.pbiomolbio.2018.03.001_bib75 article-title: Characterization of Aspergillus Niger catalase publication-title: Int. J. Biol. Macromol. doi: 10.1016/0141-8130(87)90003-1 – start-page: 137 year: 2012 ident: 10.1016/j.pbiomolbio.2018.03.001_bib97 – volume: 41 start-page: 1574 year: 1995 ident: 10.1016/j.pbiomolbio.2018.03.001_bib133 article-title: Serum catalase as marker of graft-vs-host disease in allogeneic bone marrow transplant recipients: pilot study publication-title: Clin. Chem. doi: 10.1093/clinchem/41.11.1574 – volume: 526 start-page: 54 year: 2012 ident: 10.1016/j.pbiomolbio.2018.03.001_bib46 article-title: Influence of main channel structure on H2O2 access to the heme cavity of catalase KatE of Escherichia coli publication-title: Arch. Biochem. Biophys. doi: 10.1016/j.abb.2012.06.010 – volume: 304 start-page: F1335 year: 2013 ident: 10.1016/j.pbiomolbio.2018.03.001_bib105 article-title: Overexpression of catalase prevents hypertension and tubulointerstitial fibrosis and normalization of renal angiotensin-converting enzyme-2 expression in Akita mice publication-title: Am. J. Physiol. Ren. Physiol. doi: 10.1152/ajprenal.00405.2012 – volume: 189 start-page: 201 year: 1991 ident: 10.1016/j.pbiomolbio.2018.03.001_bib73 article-title: Thermochemical analysis of Aspergillus Niger catalase and sodium n-dodecyl sulphate interaction publication-title: Thermochim. Acta doi: 10.1016/0040-6031(91)87116-E – volume: 85 start-page: 366 year: 1937 ident: 10.1016/j.pbiomolbio.2018.03.001_bib112 article-title: Crystalline catalase publication-title: Science doi: 10.1126/science.85.2206.366 – volume: 178 start-page: 1 year: 2014 ident: 10.1016/j.pbiomolbio.2018.03.001_bib106 article-title: Versatile peroxidase degradation of humic substances: use of isothermal titration calorimetry to assess kinetics, and applications to industrial wastes publication-title: J. Biotechnol. doi: 10.1016/j.jbiotec.2014.03.002 – volume: 184 start-page: 139 year: 1990 ident: 10.1016/j.pbiomolbio.2018.03.001_bib23 article-title: On the application of the Clark oxygen electrode to the study of enzyme kinetics in apolar solvents: the catalase reaction publication-title: Anal. Biochem. doi: 10.1016/0003-2697(90)90026-6 – volume: 4 year: 2012 ident: 10.1016/j.pbiomolbio.2018.03.001_bib34 article-title: Avogadro: an advanced semantic chemical editor, visualization, and analysis platform publication-title: J. Cheminf. – volume: 24 start-page: 1 year: 2004 ident: 10.1016/j.pbiomolbio.2018.03.001_bib87 article-title: Thermodynamics of protein–ligand interactions: history, presence, and future aspects publication-title: J. Recept. Signal Transduct. Res. doi: 10.1081/RRS-120037896 – year: 2016 ident: 10.1016/j.pbiomolbio.2018.03.001_bib16 – volume: 21 start-page: 257 year: 2016 ident: 10.1016/j.pbiomolbio.2018.03.001_bib138 article-title: Protective effect of an isoflavone, tectorigenin, against oxidative stress-induced cell death via catalase activation publication-title: J. Cancer Prev. doi: 10.15430/JCP.2016.21.4.257 – volume: 101 start-page: 247 year: 2004 ident: 10.1016/j.pbiomolbio.2018.03.001_bib33 article-title: Methemoglobinemia from hydrogen peroxide in a patient with acatalasemia publication-title: J. Am. Soc. Anesthesiologists – volume: 398 start-page: 1095 year: 2017 ident: 10.1016/j.pbiomolbio.2018.03.001_bib29 article-title: Catalase, a remarkable enzyme: targeting the oldest antioxidant enzyme to find a new cancer treatment approach publication-title: Biol. Chem. doi: 10.1515/hsz-2017-0131 – volume: 19 start-page: 1096 year: 1995 ident: 10.1016/j.pbiomolbio.2018.03.001_bib55 article-title: Family history of alcoholism and the mediation of alcohol intake by catalase: further evidence for catalase as a marker of the propensity to ingest alcohol publication-title: Alcohol Clin. Exp. Res. doi: 10.1111/j.1530-0277.1995.tb01586.x – volume: 19 start-page: 1292 year: 2003 ident: 10.1016/j.pbiomolbio.2018.03.001_bib118 article-title: Purification and characterization of a novel thermo-alkali-stable catalase from Thermus brockianus publication-title: Biotechnol. Prog. doi: 10.1021/bp034040t – volume: 80 start-page: 409 year: 1977 ident: 10.1016/j.pbiomolbio.2018.03.001_bib19 article-title: A more sensitive modification of the catalase assay with the Clark oxygen electrode. Application to the kinetic study of the pea leaf enzyme publication-title: Anal. Biochem. doi: 10.1016/0003-2697(77)90662-5 – volume: 39 start-page: 160 year: 2003 ident: 10.1016/j.pbiomolbio.2018.03.001_bib91 article-title: Kinetics of catalase inactivation induced by ultrasonic cavitation publication-title: Prikl. Biokhim. Mikrobiol. – volume: 61 start-page: 192 year: 2004 ident: 10.1016/j.pbiomolbio.2018.03.001_bib13 article-title: Diversity of structures and properties among catalases publication-title: Cell. Mol. Life Sci. doi: 10.1007/s00018-003-3206-5 – volume: 1777 start-page: 1032 year: 2008 ident: 10.1016/j.pbiomolbio.2018.03.001_bib79 article-title: Distance metrics for heme protein electron tunneling publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbabio.2008.04.021 – volume: 11 start-page: 26 year: 1989 ident: 10.1016/j.pbiomolbio.2018.03.001_bib76 article-title: Thermodynamics of the interaction of sodium-n-dodecyl sulphate with Aspergillus Niger catalase in high ionic strength aqueous solutions publication-title: Int. J. Biol. Macromol. doi: 10.1016/0141-8130(89)90035-4 – volume: 20 start-page: 3096 year: 1981 ident: 10.1016/j.pbiomolbio.2018.03.001_bib96 article-title: Thermodynamics of protein association reactions: forces contributing to stability publication-title: Biochemistry doi: 10.1021/bi00514a017 – volume: 59 start-page: 44 year: 2001 ident: 10.1016/j.pbiomolbio.2018.03.001_bib84 article-title: Protection against reactive oxygen species during mouse preimplantation embryo development: role of EDTA, oxygen tension, catalase, superoxide dismutase and pyruvate publication-title: Mol. Reprod. Dev. doi: 10.1002/mrd.1006 – volume: 78 start-page: 4767 year: 1981 ident: 10.1016/j.pbiomolbio.2018.03.001_bib93 article-title: Structure and heme environment of beef liver catalase at 2.5 A resolution publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.78.8.4767 – ident: 10.1016/j.pbiomolbio.2018.03.001_bib20 doi: 10.1016/j.transproceed.2005.11.083 – volume: 49 start-page: 11650 year: 2013 ident: 10.1016/j.pbiomolbio.2018.03.001_bib139 article-title: Access channel residues Ser315 and Asp137 in Mycobacterium tuberculosis catalase-peroxidase (KatG) control peroxidatic activation of the pro-drug isoniazid publication-title: Chem. Commun. doi: 10.1039/C3CC47022A – volume: 58 start-page: 148 year: 2013 ident: 10.1016/j.pbiomolbio.2018.03.001_bib58 article-title: Catalase is inhibited by flavonoids publication-title: Int. J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2013.03.070 – start-page: 611 year: 2013 ident: 10.1016/j.pbiomolbio.2018.03.001_bib41 article-title: Electron transfer in catalases and catalase-peroxidases – volume: 8 start-page: 243 year: 2006 ident: 10.1016/j.pbiomolbio.2018.03.001_bib110 article-title: Hydrogen peroxide: a signaling messenger publication-title: Antioxidants Redox Signal. doi: 10.1089/ars.2006.8.243 – volume: 51 start-page: 163 year: 1948 ident: 10.1016/j.pbiomolbio.2018.03.001_bib116 article-title: Three cases of progressive oral gangrene due to lack of catalase in the blood publication-title: Jpn. J. Otol. – volume: 82 start-page: 1604 year: 1985 ident: 10.1016/j.pbiomolbio.2018.03.001_bib24 article-title: The NADPH binding site on beef liver catalase publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.82.6.1604 – year: 2017 ident: 10.1016/j.pbiomolbio.2018.03.001_bib8 – volume: 27 start-page: 141 year: 2008 ident: 10.1016/j.pbiomolbio.2018.03.001_bib48 article-title: The interrelation of glutathione reductase, catalase, glutathione peroxidase, superoxide dismutase, and glucose-6-phosphate in the pathogenesis of rheumatoid arthritis publication-title: Clin. Rheumatol. doi: 10.1007/s10067-007-0746-3 – volume: 95 start-page: 550 year: 2017 ident: 10.1016/j.pbiomolbio.2018.03.001_bib71 article-title: Studies to reveal the nature of interactions between catalase and curcumin using computational methods and optical techniques publication-title: Int. J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2016.11.050 – volume: 171 start-page: 10 year: 2017 ident: 10.1016/j.pbiomolbio.2018.03.001_bib57 article-title: Interactions of nitrite with catalase: enzyme activity and reaction kinetics studies publication-title: J. Inorg. Biochem. doi: 10.1016/j.jinorgbio.2017.02.023 – volume: 133 start-page: 51 year: 1983 ident: 10.1016/j.pbiomolbio.2018.03.001_bib22 article-title: The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution publication-title: Eur. J. Biochem. doi: 10.1111/j.1432-1033.1983.tb07429.x – year: 2007 ident: 10.1016/j.pbiomolbio.2018.03.001_bib5 – volume: 252 start-page: 1 year: 2007 ident: 10.1016/j.pbiomolbio.2018.03.001_bib66 article-title: Dual role of hydrogen peroxide in cancer: possible relevance to cancer chemoprevention and therapy publication-title: Canc. Lett. doi: 10.1016/j.canlet.2006.10.029 – volume: 135 start-page: 15579 year: 2013 ident: 10.1016/j.pbiomolbio.2018.03.001_bib9 article-title: Water networks contribute to enthalpy/entropy compensation in protein–ligand binding publication-title: J. Am. Chem. Soc. doi: 10.1021/ja4075776 – volume: 46 start-page: 11 year: 2007 ident: 10.1016/j.pbiomolbio.2018.03.001_bib35 article-title: Relationship between the size of the bottleneck 15 A from iron in the main channel and the reactivity of catalase corresponding to the molecular size of substrates publication-title: Biochemistry doi: 10.1021/bi061519w – volume: 279 start-page: 98 year: 1998 ident: 10.1016/j.pbiomolbio.2018.03.001_bib98 article-title: Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis publication-title: Science doi: 10.1126/science.279.5347.98 – volume: 80 start-page: 2221 year: 2007 ident: 10.1016/j.pbiomolbio.2018.03.001_bib100 article-title: Hydrogen peroxide regulates the cholinergic signal in a concentration dependent manner publication-title: Life Sci. doi: 10.1016/j.lfs.2007.01.028 – volume: 489 start-page: 124 year: 2015 ident: 10.1016/j.pbiomolbio.2018.03.001_bib99 article-title: Arrhenius activation energy of damage to catalase during spray-drying publication-title: Int. J. Pharm. doi: 10.1016/j.ijpharm.2015.04.078 – volume: 6 start-page: 1395 year: 1987 ident: 10.1016/j.pbiomolbio.2018.03.001_bib17 article-title: Hydrogen peroxide in the rabbit anterior chamber: effects on glutathione, and catalase effects on peroxide kinetics publication-title: Curr. Eye Res. doi: 10.3109/02713688709044503 – year: 2016 ident: 10.1016/j.pbiomolbio.2018.03.001_bib56 – volume: 13 start-page: 869 year: 2008 ident: 10.1016/j.pbiomolbio.2018.03.001_bib25 article-title: Do enthalpy and entropy distinguish first in class from best in class? publication-title: Drug Discov. Today doi: 10.1016/j.drudis.2008.07.005 – volume: 71 start-page: 912 year: 2007 ident: 10.1016/j.pbiomolbio.2018.03.001_bib10 article-title: Catalase overexpression attenuates angiotensinogen expression and apoptosis in diabetic mice publication-title: Kidney Int. doi: 10.1038/sj.ki.5002188 – volume: 48 start-page: 1334 year: 2014 ident: 10.1016/j.pbiomolbio.2018.03.001_bib59 article-title: Flavonoid-induced conversion of catalase to its inactive form–Compound II publication-title: Free Radic. Res. doi: 10.3109/10715762.2014.953139 – volume: 17 start-page: 571 year: 2010 ident: 10.1016/j.pbiomolbio.2018.03.001_bib45 article-title: Biochemical biomarkers in environmental studies–lessons learnt from enzymes catalase, glutathione S-transferase and cholinesterase in two crustacean species publication-title: Environ. Sci. Pollut. Res. Int. doi: 10.1007/s11356-009-0112-x – volume: 279 start-page: 32804 year: 2004 ident: 10.1016/j.pbiomolbio.2018.03.001_bib38 article-title: Mice lacking catalase develop normally but show differential sensitivity to oxidant tissue injury publication-title: J. Biol. Chem. doi: 10.1074/jbc.M404800200 – year: 2005 ident: 10.1016/j.pbiomolbio.2018.03.001_bib109 |
| SSID | ssj0002176 |
| Score | 2.6222408 |
| SecondaryResourceType | review_article |
| Snippet | Catalase is one of the firsts in every realm of biological sciences. At the same time it also has a number of unusual features. It has one of the highest... |
| SourceID | proquest pubmed crossref elsevier |
| SourceType | Aggregation Database Index Database Enrichment Source Publisher |
| StartPage | 5 |
| SubjectTerms | Activity Biophysical chemistry Catalase Kinetics Mysteries Structure Thermodynamics |
| Title | Catalase and its mysteries |
| URI | https://dx.doi.org/10.1016/j.pbiomolbio.2018.03.001 https://www.ncbi.nlm.nih.gov/pubmed/29530789 https://www.proquest.com/docview/2013519699 |
| Volume | 140 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV3PS8MwFA5jIngRf7upo4LXuHRJmgZPYzim4k4Odgtpk8BkdsN1By_-7eb1x4aHgeCl0JLQ5iV932vfl-8hdNdjqeCWOUwpI5jx2OA4JBoLK4wlPuB2RTGY13E0mrDnKZ820KDeCwO0ysr3lz698NbVlW5lze5yNoM9vkJ68Ic0MvGgBbLbjAlY5fffW5qHD7mLfKVvjKF1xeYpOV5L2OO-mPsjkLziUu403AVRu0LQAoqGR-iwiiGDfvmYx6hhsxO0X1aV_DpF7QH8kvHoFOjMBLN8FXyAXDN8E5-hyfDxbTDCVQkEnFLBcpxyx7VOvAmNDLVLEx3qyAkPuynh2rLIo3PPCBI7Czr1IaQJTRTr1FGpiUnpOWpmi8xe-lFrLhMuLaNCM2kSHRtifPzmDKVG6rCFRD1qlVb64FCmYq5qIti72tpLgb0UocCJa6Fw03NZamT8oc9DbVj1a76Vd-V_6H1bz4XyrwPkOHRmF-sVNIKSg5GULXRRTtLmmXqSU1DXb__r3lfoAM5KSss1auafa3vjA5M86RQrr4P2-k8vo_EP9SLhPw |
| linkProvider | Elsevier |
| linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1Lb8IwDLYYaNou096DvZi0a7WUJE2jnRAagvE4gcQtSptUYmIFDTjs3y-mLdMOSEi79NDGauK0tlt__gzw3GCx4JYlHqWMeIyHxgt9oj1hhbHEBdzJphnMYBh0xux9wiclaBW1MAirzG1_ZtM31jo_85Jr82UxnWKNr5DO-WMamTinFRxABdmpeBkqzW6vM9waZBd1b1KWbryHAjmgJ4N5LbDMfT5zR8R5hRnjqb_LS-2KQjfeqH0KJ3kYWW9mMz2Dkk3P4TBrLPl9AbUW_pVxDqquU1Ofrpb1T2Rsxs_iSxi330atjpd3QfBiKtjKi3nCtY6cFo30dRJH2tdBIpznjQnXlgXOQTeMIGFikarex0yhCUIdJ1RqYmJ6BeV0ntobt2rNZcSlZVRoJk2kQ0OMC-ESQ6mR2q-CKFat4pwiHDtVzFSBBftQv_pSqC9FKMLiquBvJRcZTcYeMq-FYtWfLVfOmu8h_VTshXJvBKY5dGrn6yUOwq6DgZRVuM42aTunhuQUCfZr_7r3Ixx1RoO-6neHvVs4xisZwuUOyquvtb13ccoqesifwx-3XOPw |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Catalase+and+its+mysteries&rft.jtitle=Progress+in+biophysics+and+molecular+biology&rft.au=Sepasi+Tehrani%2C+Hessam&rft.au=Moosavi-Movahedi%2C+Ali+Akbar&rft.date=2018-12-01&rft.eissn=1873-1732&rft.volume=140&rft.spage=5&rft_id=info:doi/10.1016%2Fj.pbiomolbio.2018.03.001&rft_id=info%3Apmid%2F29530789&rft.externalDocID=29530789 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0079-6107&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0079-6107&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0079-6107&client=summon |