Computational modeling of the direct hydride transfer mechanism for the MAO catalyzed oxidation of phenethylamine and benzylamine: ONIOM (QM/QM) calculations
Monoamine oxidases are two isozymic flavoenzymes which are the important targets for drugs used in the treatment of depression, Parkinson and Alzheimer’s diseases. The catalytic reaction taking place between the cofactor FAD and amine substrate is still not completely understood. Herein we employed...
Saved in:
| Published in | Journal of Neural Transmission Vol. 120; no. 6; pp. 937 - 945 |
|---|---|
| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
Vienna
Springer Vienna
01.06.2013
Springer Nature B.V |
| Subjects | |
| Online Access | Get full text |
Cover
Loading…
| Abstract | Monoamine oxidases are two isozymic flavoenzymes which are the important targets for drugs used in the treatment of depression, Parkinson and Alzheimer’s diseases. The catalytic reaction taking place between the cofactor FAD and amine substrate is still not completely understood. Herein we employed quantum chemical methods on the recently proposed direct hydride transfer mechanism including full active site residues of MAO isoforms in the calculations. Activation free energy barriers of direct hydride transfer mechanism for MAO-A and MAO-B were calculated by ONIOM (our own
n
-layered integrated molecular orbital + molecular mechanics) method with QM/QM (quantum mechanics:quantum mechanics) approach employing several density functional theory functionals, B3LYP, WB97XD, CAM-B3LYP and M06-2X, for the high layer. The formation of very recently proposed αC–flavin N5 adduct inside the enzyme has been investigated. ONIOM (M06-2X/6-31+G(d,p):PM6) results revealed that such an adduct may form only in MAO-B suggesting slightly different hydride transfer mechanisms for MAO-A and MAO-B. |
|---|---|
| AbstractList | Monoamine oxidases are two isozymic flavoenzymes which are the important targets for drugs used in the treatment of depression, Parkinson and Alzheimer's diseases. The catalytic reaction taking place between the cofactor FAD and amine substrate is still not completely understood. Herein we employed quantum chemical methods on the recently proposed direct hydride transfer mechanism including full active site residues of MAO isoforms in the calculations. Activation free energy barriers of direct hydride transfer mechanism for MAO-A and MAO-B were calculated by ONIOM (our own n-layered integrated molecular orbital + molecular mechanics) method with QM/QM (quantum mechanics:quantum mechanics) approach employing several density functional theory functionals, B3LYP, WB97XD, CAM-B3LYP and M06-2X, for the high layer. The formation of very recently proposed αC-flavin N5 adduct inside the enzyme has been investigated. ONIOM (M06-2X/6-31+G(d,p):PM6) results revealed that such an adduct may form only in MAO-B suggesting slightly different hydride transfer mechanisms for MAO-A and MAO-B. Issue Title: Special Issue: 15th Amine Oxidase Conference: Re-Examining Amines Monoamine oxidases are two isozymic flavoenzymes which are the important targets for drugs used in the treatment of depression, Parkinson and Alzheimer's diseases. The catalytic reaction taking place between the cofactor FAD and amine substrate is still not completely understood. Herein we employed quantum chemical methods on the recently proposed direct hydride transfer mechanism including full active site residues of MAO isoforms in the calculations. Activation free energy barriers of direct hydride transfer mechanism for MAO-A and MAO-B were calculated by ONIOM (our own n-layered integrated molecular orbital + molecular mechanics) method with QM/QM (quantum mechanics:quantum mechanics) approach employing several density functional theory functionals, B3LYP, WB97XD, CAM-B3LYP and M06-2X, for the high layer. The formation of very recently proposed [alpha]C-flavin N5 adduct inside the enzyme has been investigated. ONIOM (M06-2X/6-31+G(d,p):PM6) results revealed that such an adduct may form only in MAO-B suggesting slightly different hydride transfer mechanisms for MAO-A and MAO-B.[PUBLICATION ABSTRACT] Monoamine oxidases are two isozymic flavoenzymes which are the important targets for drugs used in the treatment of depression, Parkinson and Alzheimer's diseases. The catalytic reaction taking place between the cofactor FAD and amine substrate is still not completely understood. Herein we employed quantum chemical methods on the recently proposed direct hydride transfer mechanism including full active site residues of MAO isoforms in the calculations. Activation free energy barriers of direct hydride transfer mechanism for MAO-A and MAO-B were calculated by ONIOM (our own n-layered integrated molecular orbital + molecular mechanics) method with QM/QM (quantum mechanics:quantum mechanics) approach employing several density functional theory functionals, B3LYP, WB97XD, CAM-B3LYP and M06-2X, for the high layer. The formation of very recently proposed alpha C-flavin N5 adduct inside the enzyme has been investigated. ONIOM (M06-2X/6-31+G(d,p):PM6) results revealed that such an adduct may form only in MAO-B suggesting slightly different hydride transfer mechanisms for MAO-A and MAO-B. Monoamine oxidases are two isozymic flavoenzymes which are the important targets for drugs used in the treatment of depression, Parkinson and Alzheimer’s diseases. The catalytic reaction taking place between the cofactor FAD and amine substrate is still not completely understood. Herein we employed quantum chemical methods on the recently proposed direct hydride transfer mechanism including full active site residues of MAO isoforms in the calculations. Activation free energy barriers of direct hydride transfer mechanism for MAO-A and MAO-B were calculated by ONIOM (our own n -layered integrated molecular orbital + molecular mechanics) method with QM/QM (quantum mechanics:quantum mechanics) approach employing several density functional theory functionals, B3LYP, WB97XD, CAM-B3LYP and M06-2X, for the high layer. The formation of very recently proposed αC–flavin N5 adduct inside the enzyme has been investigated. ONIOM (M06-2X/6-31+G(d,p):PM6) results revealed that such an adduct may form only in MAO-B suggesting slightly different hydride transfer mechanisms for MAO-A and MAO-B. |
| Author | Erdem, Safiye Sağ Akyüz, Mehmet Ali |
| Author_xml | – sequence: 1 givenname: Mehmet Ali surname: Akyüz fullname: Akyüz, Mehmet Ali organization: Department of Chemistry, Faculty of Arts and Sciences, Marmara University – sequence: 2 givenname: Safiye Sağ surname: Erdem fullname: Erdem, Safiye Sağ email: erdem@marmara.edu.tr organization: Department of Chemistry, Faculty of Arts and Sciences, Marmara University |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/23619993$$D View this record in MEDLINE/PubMed |
| BookMark | eNqNkV1rFDEUhoNU7Lb6A7yRgDftxdiTSWYy8a4sVgtdl4JeD5nkTCdlJlmTGXD7X_yvzn4oIgjeJITzvM-BvGfkxAePhLxm8I4ByKs0H5BnwHjGIJdZ9YwsmOBFxkTJT8gCOECmilKckrOUHgGAMVm9IKc5L5lSii_Ij2UYNtOoRxe87ukQLPbOP9DQ0rFDal1EM9Jua6OzSMeofWox0gFNp71LA21D3JOr6zU1etT99gktDd-d3Tt3ok2HHsdu2-vBeaTaW9qgfzq-39P159v1il7cr67uV5ezpDdTvw-nl-R5q_uEr473Ofl68-HL8lN2t_54u7y-y4yQbMyQcWkqlbfQQlUoXUGhUKIprckRbGOM0KIRquGyEqXWylZazgPbNiALzPk5uTh4NzF8mzCN9eCSwb7XHsOUasZLKRQv8_I_0KLkigGXM_r2L_QxTHH-5j1V8FxxVs0UO1AmhpQitvUmukHHbc2g3tVcH2qu55rrXc31LvPmaJ6aAe3vxK9eZyA_AGke-QeMf6z-p_Un7Sm1mw |
| CODEN | JNTRF3 |
| CitedBy_id | crossref_primary_10_1016_j_bioorg_2018_02_003 crossref_primary_10_1371_journal_pone_0290901 crossref_primary_10_1016_j_tet_2017_07_040 crossref_primary_10_1039_D0CP00131G crossref_primary_10_1021_acs_jcim_2c00569 crossref_primary_10_1002_prot_25374 crossref_primary_10_1021_acs_jpcb_6b09011 crossref_primary_10_1002_cphc_202300431 crossref_primary_10_1039_C7CP07069A crossref_primary_10_3390_ijms23031910 crossref_primary_10_1007_s11164_018_03721_z crossref_primary_10_1039_C6CP00098C crossref_primary_10_1039_D1CP03993H crossref_primary_10_1021_acs_jpcb_0c06502 crossref_primary_10_1038_s41598_022_26296_7 crossref_primary_10_1002_med_21561 crossref_primary_10_1039_C6RA27894A crossref_primary_10_1039_c3ob42388c crossref_primary_10_1007_s11224_022_02092_x crossref_primary_10_1016_j_ejphar_2017_05_061 crossref_primary_10_1039_C6OB01175F crossref_primary_10_1021_acsami_5b10528 crossref_primary_10_1016_j_molstruc_2016_02_055 crossref_primary_10_4155_fmc_14_23 crossref_primary_10_1002_prot_24690 crossref_primary_10_1021_jp4061522 crossref_primary_10_3390_molecules27196711 crossref_primary_10_3389_fnins_2016_00327 crossref_primary_10_1021_acs_jpcb_6b00894 crossref_primary_10_1021_acsomega_3c01949 crossref_primary_10_1016_j_compbiolchem_2013_08_007 crossref_primary_10_1002_slct_202203319 crossref_primary_10_1021_acscatal_8b04045 crossref_primary_10_1039_D0OB01118E crossref_primary_10_1021_acsomega_1c03357 crossref_primary_10_1016_j_molstruc_2023_137247 crossref_primary_10_1021_acsomega_4c00307 crossref_primary_10_1007_s00702_018_1861_9 crossref_primary_10_1021_jp500795p crossref_primary_10_1021_acs_biochem_9b00213 crossref_primary_10_3390_chemistry3030069 crossref_primary_10_1039_C6CP08172J crossref_primary_10_1021_jp512470a crossref_primary_10_1021_cr5004419 crossref_primary_10_3389_fchem_2018_00169 crossref_primary_10_1007_s00894_020_04646_4 crossref_primary_10_1016_j_comptc_2022_113789 crossref_primary_10_1002_chem_201605430 crossref_primary_10_1021_acs_jcim_5b00140 |
| Cites_doi | 10.1007/s00894-007-0233-4 10.1007/s00775-012-0888-x 10.1021/ja205629b 10.1021/bi020309q 10.1039/b810189b 10.1021/bi700482h 10.1021/bi00253a026 10.1007/s00702-007-0670-3 10.1007/s00702-011-0635-4 10.1016/j.cplett.2004.06.011 10.1073/pnas.0505975102 10.2174/0929867043364784 10.1007/s00214-007-0310-x 10.1021/ct200031t 10.1039/b511350d 10.1016/S0166-1280(98)00475-8 10.1073/pnas.1633804100 10.1021/jp0619181 10.1002/jcc.23112 10.1016/S0166-1280(01)00587-5 10.1016/j.abb.2009.07.019 10.1021/j100091a024 10.1073/pnas.0710626105 10.1021/bi200951z 10.1021/bi990920y 10.1007/s00702-007-0678-8 10.1063/1.464304 10.1021/ct9000922 10.1103/PhysRevB.37.785 10.1021/bi001957h 10.1021/jp0734474 10.1002/cbic.201000184 10.1002/ejoc.201201122 |
| ContentType | Journal Article |
| Copyright | Springer-Verlag Wien 2013 |
| Copyright_xml | – notice: Springer-Verlag Wien 2013 |
| DBID | CGR CUY CVF ECM EIF NPM AAYXX CITATION K9. 7X8 7TK |
| DOI | 10.1007/s00702-013-1027-8 |
| DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef ProQuest Health & Medical Complete (Alumni) MEDLINE - Academic Neurosciences Abstracts |
| DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef ProQuest Health & Medical Complete (Alumni) MEDLINE - Academic Neurosciences Abstracts |
| DatabaseTitleList | MEDLINE ProQuest Health & Medical Complete (Alumni) Neurosciences Abstracts |
| 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 – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Medicine Anatomy & Physiology |
| EISSN | 1435-1463 |
| EndPage | 945 |
| ExternalDocumentID | 2979690291 10_1007_s00702_013_1027_8 23619993 |
| Genre | Research Support, Non-U.S. Gov't Journal Article |
| GroupedDBID | -53 -BR 1SB 28- 29L 29~ 3SX 40D 40E 5QI 5RE 95- 95. 95~ ABMNI AEFIE AGWIL ALMA_UNASSIGNED_HOLDINGS BBWZM F5P LAS O93 O9G O9I O9J P19 QOK RHV RNI ROL RZK SDE SOJ WK6 ~EX -5G -EM -~C .VR 06C 2.D 2J2 2JN 2JY 2KG 2KM 2LR 2VQ 2~H 406 408 409 53G 67Z 8TC 8UJ 96X AABHQ AATVU AAUYE AAWCG AAYTO ABBBX ABBXA ABHQN ABIPD ABJNI ABLJU ABWNU ACBXY ACOMO ACREN ADIMF ADINQ ADJJI ADKNI ADQRH AEGAL AEGNC AEXYK AFBBN AFQWF AGAYW AHBYD AHYZX AJRNO AMYLF B-. BA0 CAG CGR COF CUY CVF EBS ECM EIF EN4 FEDTE FNLPD G-Y G-Z GGCAI GQ6 GQ7 GQ8 GXS HG5 HG6 HVGLF IJ- IMOTQ ITM IXC I~Z J-C KDC KOV KPH MA- NB0 NPM OAM P9S PF0 Q2X QOR QOS R89 RNS RRX RSV S16 S27 S37 S3B SAP SDH SHX SMD SNE SNX SZ9 SZN T13 TSG TUC U2A U9L VC2 W23 W48 Z45 AAYXX CITATION --- -5E .86 06D 0R~ 0VY 1N0 203 30V 36B 4.4 5VS 6NX 78A AAAVM AACDK AAHNG AAIAL AAJBT AAJKR AANXM AANZL AARHV AARTL AASML AATNV AAYIU AAYQN ABAKF ABDZT ABECU ABFTV ABHLI ABIVO ABJOX ABKCH ABKTR ABMQK ABNWP ABPLI ABQBU ABSXP ABTEG ABTKH ABTMW ABULA ABXPI ACAOD ACDTI ACGFO ACGFS ACHSB ACHXU ACIPQ ACKNC ACMDZ ACMLO ACOKC ACZOJ ADHHG ADHIR ADKPE ADRFC ADTPH ADURQ ADYFF ADYOE ADZKW AEBTG AEFQL AEGXH AEJHL AEJRE AEKMD AEMSY AENEX AEOHA AEPYU AESKC AETLH AEVLU AFLOW AFWTZ AFYQB AFZKB AGDGC AGJBK AGMZJ AGQEE AGQMX AGRTI AGWZB AGYKE AHIZS AHKAY AHMBA AHSBF AIAGR AIAKS AIGIU AIIXL AILAN AITGF AJBLW AJZVZ AKMHD ALWAN AMKLP AMTXH AMXSW AMYQR AOCGG ARMRJ AXYYD AZFZN BDATZ BGNMA CSCUP DDRTE DL5 DNIVK DPUIP DU5 EBD EBLON EIOEI EJD EMB EMOBN EPAXT ESBYG FERAY FFXSO FIGPU FINBP FRRFC FSGXE FWDCC GGRSB GJIRD GNWQR H13 HF~ HMJXF HQYDN HRMNR HZ~ I09 IHE IKXTQ IWAJR IZIGR IZQ I~X J0Z JBSCW JCJTX JZLTJ K9. LLZTM M4Y N2Q N9A NPVJJ NQJWS NU0 O9- P2P PQQKQ PT4 PT5 R9I RPX SCLPG SDM SISQX SJYHP SNPRN SOHCF SPISZ SRMVM SSLCW SSXJD SV3 TSK TSV TT1 UG4 UOJIU UTJUX UZXMN VFIZW WJK WK8 YLTOR Z7U Z82 Z83 Z87 Z8O Z8V Z8W Z91 ZMTXR ZOVNA 7X8 7TK |
| ID | FETCH-LOGICAL-c471t-e137c892f0f0859a8059e7ec6dc2e0dbcc4a4b49b37846aa9d8a7e0ddfb075e23 |
| IEDL.DBID | U2A |
| ISSN | 0300-9564 |
| IngestDate | Fri Oct 25 05:45:06 EDT 2024 Fri Jun 28 08:48:23 EDT 2024 Thu Oct 10 16:05:57 EDT 2024 Fri Aug 23 04:06:22 EDT 2024 Wed Mar 20 10:39:56 EDT 2024 Sat Dec 16 12:00:53 EST 2023 |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 6 |
| Keywords | Dispersion-corrected DFT Hydride transfer Enzyme modeling Enzyme mechanism Flavoenzymes |
| Language | English |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c471t-e137c892f0f0859a8059e7ec6dc2e0dbcc4a4b49b37846aa9d8a7e0ddfb075e23 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 ObjectType-Article-2 ObjectType-Feature-1 |
| PMID | 23619993 |
| PQID | 1355329318 |
| PQPubID | 51646 |
| PageCount | 9 |
| ParticipantIDs | proquest_miscellaneous_1367493626 proquest_miscellaneous_1356391037 proquest_journals_1355329318 crossref_primary_10_1007_s00702_013_1027_8 pubmed_primary_23619993 springer_journals_10_1007_s00702_013_1027_8 |
| PublicationCentury | 2000 |
| PublicationDate | 2013-06-01 |
| PublicationDateYYYYMMDD | 2013-06-01 |
| PublicationDate_xml | – month: 06 year: 2013 text: 2013-06-01 day: 01 |
| PublicationDecade | 2010 |
| PublicationPlace | Vienna |
| PublicationPlace_xml | – name: Vienna – name: Austria – name: Wien |
| PublicationSubtitle | Translational Neuroscience, Neurology and Preclinical Neurological Studies, Psychiatry and Preclinical Psychiatric Studies |
| PublicationTitle | Journal of Neural Transmission |
| PublicationTitleAbbrev | J Neural Transm |
| PublicationTitleAlternate | J Neural Transm (Vienna) |
| PublicationYear | 2013 |
| Publisher | Springer Vienna Springer Nature B.V |
| Publisher_xml | – name: Springer Vienna – name: Springer Nature B.V |
| References | Kim, Jordan (CR18) 1994; 98 Prabhakar, Vreven, Frisch, Morokuma, Musaev (CR26) 2006; 110 Wang, Edmondson (CR36) 2011; 50 CR15 CR34 Yuan, Jijun, Fengyu, Zhongfang (CR38) 2013; 34 Silverman, Mariano (CR29) 1992 Nandigama, Edmondson (CR25) 2000; 39 Chai, Head-Gordon (CR4) 2008; 10 Zhao, Truhlar (CR39) 2008; 120 Jonsson, Edmondson, Klinman (CR17) 1994; 33 Lu, Rodrigez, Silverman, Vintem, Ramsay, Chapman, Perham, Scrutton (CR22) 2002 Wang, Edmondson (CR35) 2007; 114 Binda, Li, Hubálek, Restelli, Edmondson, Mattevi (CR3) 2003; 100 Rezac, Fanfrlik, Salahub, Hobza (CR28) 2009; 5 Ertem, Cramer, Himo, Siegbahn (CR13) 2012; 17 Miller, Edmondson (CR24) 1999; 38 Tilocca, Gamba, Vanoni, Fois (CR33) 2002; 41 MacMillar, Edmondson, Matsson (CR23) 2011; 133 Ralph, Hirschi, Anderson, Cleland, Singleton, Fitzpatrick (CR27) 2007; 46 Son, Ma, Kondou, Yoshimura, Yamashita, Tsukihara (CR30) 2008; 105 Edmondson, Mattevi, Binda, Li, Hubálek (CR8) 2004; 11 Erdem, Yelekçi (CR10) 2001; 572 Kong, Ouyang, Liang, Lu, Chen, Shen, Li, Zheng, Li, Luo, Jiang (CR19) 2011; 6 Yanai, Tew, Handy (CR37) 2004; 393 Fitzpatrick (CR14) 2010; 493 Dunn, Munro, Turner, Rigby, Scrutton (CR7) 2010; 11 Erdem, Büyükmenekşe (CR9) 2011; 118 Colibus, Binda, Lustig, Edmondson, Mattevi (CR5) 2005; 102 Erdem, Karahan, Yıldız, Yelekçi (CR11) 2006; 4 Sousa, Fernandes, Ramos (CR31) 2007; 111 Erdem, Altınbaş, Boz (CR12) 2013 Lee, Yang, Parr (CR20) 1988; 37–2 Becke (CR2) 1993; 98–2 Liao, Yu, Himo (CR21) 2011; 7 Dapprich, Komaromi, Byun, Morokuma, Frisch (CR6) 1999; 461–462 Akyüz, Erdem, Edmondson (CR1) 2007; 114 Stewart (CR32) 2007; 13 26610140 - J Chem Theory Comput. 2011 May 10;7(5):1494-501 18391214 - Proc Natl Acad Sci U S A. 2008 Apr 15;105(15):5739-44 17542620 - Biochemistry. 2007 Jun 26;46(25):7655-64 12913124 - Proc Natl Acad Sci U S A. 2003 Aug 19;100(17):9750-5 7993913 - Biochemistry. 1994 Dec 13;33(49):14871-8 21819071 - Biochemistry. 2011 Sep 6;50(35):7710-7 10521274 - Biochemistry. 1999 Oct 12;38(41):13670-83 21476070 - J Neural Transm (Vienna). 2011 Jul;118(7):1021-9 22434248 - J Biol Inorg Chem. 2012 Jun;17(5):687-98 15279562 - Curr Med Chem. 2004 Aug;11(15):1983-93 26610000 - J Chem Theory Comput. 2009 Jul 14;5(7):1749-60 17718548 - J Phys Chem A. 2007 Oct 25;111(42):10439-52 12450374 - Biochemistry. 2002 Dec 3;41(48):14111-21 17401534 - J Neural Transm (Vienna). 2007;114(6):721-4 16821888 - J Phys Chem B. 2006 Jul 13;110(27):13608-13 21984927 - PLoS One. 2011;6(9):e25444 18989472 - Phys Chem Chem Phys. 2008 Nov 28;10(44):6615-20 21786798 - J Am Chem Soc. 2011 Aug 17;133(32):12319-21 11106506 - Biochemistry. 2000 Dec 12;39(49):15258-65 17401536 - J Neural Transm (Vienna). 2007;114(6):693-8 19651103 - Arch Biochem Biophys. 2010 Jan 1;493(1):13-25 16129825 - Proc Natl Acad Sci U S A. 2005 Sep 6;102(36):12684-9 23323992 - J Enzyme Inhib Med Chem. 2014 Feb;29(1):81-6 9944570 - Phys Rev B Condens Matter. 1988 Jan 15;37(2):785-789 20480485 - Chembiochem. 2010 Jun 14;11(9):1228-31 22949382 - J Comput Chem. 2013 Jan 15;34(2):121-31 16467939 - Org Biomol Chem. 2006 Feb 21;4(4):646-58 17828561 - J Mol Model. 2007 Dec;13(12):1173-213 J Rezac (1027_CR28) 2009; 5 RV Dunn (1027_CR7) 2010; 11 T Yanai (1027_CR37) 2004; 393 JD Chai (1027_CR4) 2008; 10 S MacMillar (1027_CR23) 2011; 133 Y Zhao (1027_CR39) 2008; 120 PF Fitzpatrick (1027_CR14) 2010; 493 J Wang (1027_CR36) 2011; 50 JJP Stewart (1027_CR32) 2007; 13 A Tilocca (1027_CR33) 2002; 41 MA Akyüz (1027_CR1) 2007; 114 EC Ralph (1027_CR27) 2007; 46 SY Son (1027_CR30) 2008; 105 RB Silverman (1027_CR29) 1992 R-Z Liao (1027_CR21) 2011; 7 J Wang (1027_CR35) 2007; 114 K Kim (1027_CR18) 1994; 98 RK Nandigama (1027_CR25) 2000; 39 X Lu (1027_CR22) 2002 DE Edmondson (1027_CR8) 2004; 11 AD Becke (1027_CR2) 1993; 98–2 C Binda (1027_CR3) 2003; 100 LD Colibus (1027_CR5) 2005; 102 C Lee (1027_CR20) 1988; 37–2 X Kong (1027_CR19) 2011; 6 SS Erdem (1027_CR9) 2011; 118 SS Erdem (1027_CR12) 2013 S Dapprich (1027_CR6) 1999; 461–462 SS Erdem (1027_CR10) 2001; 572 MZ Ertem (1027_CR13) 2012; 17 1027_CR15 SS Erdem (1027_CR11) 2006; 4 JR Miller (1027_CR24) 1999; 38 R Prabhakar (1027_CR26) 2006; 110 1027_CR34 SF Sousa (1027_CR31) 2007; 111 T Jonsson (1027_CR17) 1994; 33 L Yuan (1027_CR38) 2013; 34 |
| References_xml | – volume: 13 start-page: 1173 year: 2007 end-page: 1213 ident: CR32 article-title: Optimization of parameters for semiempirical methods. V. Modification of NDDO approximations and application to 70 elements publication-title: J Mol Model doi: 10.1007/s00894-007-0233-4 contributor: fullname: Stewart – volume: 17 start-page: 687 year: 2012 end-page: 698 ident: CR13 article-title: N–O bond cleavage mechanism(s) in nitrous oxide reductase publication-title: J Biol Inorg Chem doi: 10.1007/s00775-012-0888-x contributor: fullname: Siegbahn – volume: 133 start-page: 12319 year: 2011 end-page: 12321 ident: CR23 article-title: Nitrogen kinetic isotope effects for the monoamine oxidase B-catalyzed oxidation of benzylamine and (1,1-2H2) benzylamine: nitrogen rehybridization and CH bond cleavage are not concerted publication-title: J Am Chem Soc doi: 10.1021/ja205629b contributor: fullname: Matsson – volume: 41 start-page: 14111 year: 2002 end-page: 14121 ident: CR33 article-title: First-principles molecular dynamics investigation of the d-amino acid oxidative half-reaction catalyzed by the flavoenzyme -amino acid oxidase publication-title: Biochemistry doi: 10.1021/bi020309q contributor: fullname: Fois – volume: 10 start-page: 6615 year: 2008 end-page: 6620 ident: CR4 article-title: Long-range corrected hybrid density functionals with damped atom–atom dispersion corrections publication-title: Phys Chem Chem Phys doi: 10.1039/b810189b contributor: fullname: Head-Gordon – volume: 46 start-page: 7655 year: 2007 end-page: 7664 ident: CR27 article-title: Insight into the mechanism of flavoprotein-catalyzed amine oxidation from nitrogen isotope effect on the reaction of -methyltryptophan oxidase publication-title: Biochemistry doi: 10.1021/bi700482h contributor: fullname: Fitzpatrick – volume: 33 start-page: 14871 year: 1994 end-page: 14878 ident: CR17 article-title: Hydrogen tunneling in the flavoenzyme monoamine oxidase B publication-title: Biochemistry doi: 10.1021/bi00253a026 contributor: fullname: Klinman – volume: 114 start-page: 693 year: 2007 end-page: 698 ident: CR1 article-title: The aromatic cage in the active site of monoamine oxidase B: effect on the structural and electronic properties of bound benzylamine and -nitrobenzylamine publication-title: J Neural Transm doi: 10.1007/s00702-007-0670-3 contributor: fullname: Edmondson – volume: 118 start-page: 1021 year: 2011 end-page: 1029 ident: CR9 article-title: Computational investigation on the structure–activity relationship of the biradical mechanism for monoamine oxidase publication-title: J Neural Transm doi: 10.1007/s00702-011-0635-4 contributor: fullname: Büyükmenekşe – volume: 393 start-page: 51 year: 2004 end-page: 57 ident: CR37 article-title: New hybrid exchange–correlation functional using the Coulomb-attenuating method (CAM-B3LYP) publication-title: Chem Phys Lett doi: 10.1016/j.cplett.2004.06.011 contributor: fullname: Handy – volume: 102 start-page: 12684 year: 2005 end-page: 12689 ident: CR5 article-title: Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B publication-title: Proc Natl Acad Sci doi: 10.1073/pnas.0505975102 contributor: fullname: Mattevi – volume: 11 start-page: 1983 year: 2004 end-page: 1993 ident: CR8 article-title: Structure and mechanism of monoamine oxidase publication-title: Curr Med Chem doi: 10.2174/0929867043364784 contributor: fullname: Hubálek – volume: 120 start-page: 215 year: 2008 end-page: 241 ident: CR39 article-title: The M06 suite of density functionals for main group thermochemistry, thermochemical kinetics, noncovalent interactions, excited states, and transition elements: two new functionals and systematic testing of four M06-class functionals and 12 other functional publication-title: Theor Chem Acc doi: 10.1007/s00214-007-0310-x contributor: fullname: Truhlar – volume: 7 start-page: 1494 year: 2011 end-page: 1501 ident: CR21 article-title: Quantum chemical modeling of enzymatic reactions: the case of decarboxylation publication-title: J Chem Theory Comput doi: 10.1021/ct200031t contributor: fullname: Himo – volume: 4 start-page: 646 year: 2006 end-page: 658 ident: CR11 article-title: A computational study on the amine-oxidation mechanism of monoamine oxidase: insight into the polar nucleophilic mechanism publication-title: Org Biomol Chem doi: 10.1039/b511350d contributor: fullname: Yelekçi – start-page: 177 year: 1992 end-page: 213 ident: CR29 article-title: Electron transfer chemistry of monoamine oxidase publication-title: Advances in electron transfer chemistry contributor: fullname: Mariano – volume: 461–462 start-page: 1 year: 1999 end-page: 21 ident: CR6 article-title: A new ONIOM implementation in Gaussian98. Part I. The calculation of energies, gradients, vibrational frequencies and electric field derivatives publication-title: J Mol Struct (Theochem) doi: 10.1016/S0166-1280(98)00475-8 contributor: fullname: Frisch – volume: 100 start-page: 9750 year: 2003 end-page: 9755 ident: CR3 article-title: Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures publication-title: Proc Natl Acad Sci doi: 10.1073/pnas.1633804100 contributor: fullname: Mattevi – volume: 110 start-page: 13608 year: 2006 end-page: 13613 ident: CR26 article-title: Is the protein surrounding the active site critical for hydrogen peroxide reduction by selenoprotein glutathione peroxidase? An ONIOM study publication-title: J Phys Chem B doi: 10.1021/jp0619181 contributor: fullname: Musaev – volume: 34 start-page: 121 year: 2013 end-page: 131 ident: CR38 article-title: Appropriate description of intermolecular interactions in the methane hydrates: an assessment of DFT methods publication-title: J Comput Chem doi: 10.1002/jcc.23112 contributor: fullname: Zhongfang – volume: 572 start-page: 97 year: 2001 end-page: 106 ident: CR10 article-title: Computer modeling of oxygen containing heptylamines as monoamine oxidase inactivators publication-title: J Mol Struct (Theochem) doi: 10.1016/S0166-1280(01)00587-5 contributor: fullname: Yelekçi – volume: 493 start-page: 13 year: 2010 end-page: 25 ident: CR14 article-title: Oxidation of amines by flavoproteins publication-title: Arch Biochem Biophys doi: 10.1016/j.abb.2009.07.019 contributor: fullname: Fitzpatrick – volume: 98 start-page: 10089 year: 1994 end-page: 10094 ident: CR18 article-title: Comparison of density functional and MP2 calculations on the water monomer and dimer publication-title: J Phys Chem doi: 10.1021/j100091a024 contributor: fullname: Jordan – volume: 105 start-page: 5739 year: 2008 end-page: 5744 ident: CR30 article-title: Structure of human monoamine oxidase A at 2.2-Å resolution: the control of opening the entry for substrates/inhibitors publication-title: Proc Natl Acad Sci doi: 10.1073/pnas.0710626105 contributor: fullname: Tsukihara – volume: 50 start-page: 7710 year: 2011 end-page: 7717 ident: CR36 article-title: 2H Kinetic isotope effects and pH dependence of catalysis as mechanistic probes of rat monoamine oxidase A: comparisons with the human enzyme publication-title: Biochemistry doi: 10.1021/bi200951z contributor: fullname: Edmondson – ident: CR15 – volume: 38 start-page: 13670 year: 1999 end-page: 13683 ident: CR24 article-title: Structure-activity relationships in the oxidation of para-substituted benzylamine analogues by recombinant human liver monoamine oxidase A publication-title: Biochemistry doi: 10.1021/bi990920y contributor: fullname: Edmondson – volume: 114 start-page: 721 year: 2007 end-page: 724 ident: CR35 article-title: Do monomeric vs dimeric forms of MAO-A make a difference? A direct comparison of the catalytic properties of rat and human MAO-A’s publication-title: J Neural Transm doi: 10.1007/s00702-007-0678-8 contributor: fullname: Edmondson – volume: 98–2 start-page: 1372 year: 1993 end-page: 1377 ident: CR2 article-title: A new mixing of Hartree–Fock and local density-functional theories publication-title: J Chem Phys doi: 10.1063/1.464304 contributor: fullname: Becke – volume: 5 start-page: 1749 year: 2009 end-page: 1760 ident: CR28 article-title: Semiempirical quantum chemical PM6 method augmented by dispersion and H-bonding correction terms reliably describes various types of noncovalent complexes publication-title: J Chem Theory Comput doi: 10.1021/ct9000922 contributor: fullname: Hobza – volume: 37–2 start-page: 785 year: 1988 end-page: 789 ident: CR20 article-title: Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density publication-title: Phys Rev B doi: 10.1103/PhysRevB.37.785 contributor: fullname: Parr – ident: CR34 – volume: 39 start-page: 15258 year: 2000 end-page: 15265 ident: CR25 article-title: Structure–activity relations in the oxidation of phenethylamine analogues by recombinant human liver monoamine oxidase A publication-title: Biochemistry doi: 10.1021/bi001957h contributor: fullname: Edmondson – volume: 6 start-page: 1 year: 2011 end-page: 11 ident: CR19 article-title: Catalytic mechanism investigation of lysine-specific demethylase 1 (LSD1): a computational study publication-title: PLoS ONE contributor: fullname: Jiang – year: 2013 ident: CR12 article-title: Quantum chemical modeling of the inhibition mechanism of monoamine oxidase by oxazolidinone and analogous heterocyclic compounds publication-title: J Enzyme Inhib Med Chem contributor: fullname: Boz – volume: 111 start-page: 10439 year: 2007 end-page: 10452 ident: CR31 article-title: General performance of density functionals publication-title: J Phys Chem A doi: 10.1021/jp0734474 contributor: fullname: Ramos – start-page: 817 year: 2002 ident: CR22 article-title: Irreversible inactivation of mitochondrial monoamine oxidase publication-title: Flavins and flavoproteins contributor: fullname: Scrutton – volume: 11 start-page: 1228 year: 2010 end-page: 1231 ident: CR7 article-title: Tyrosyl radical formation and propagation in flavin dependent monoamine oxidases publication-title: Chem Bio Chem doi: 10.1002/cbic.201000184 contributor: fullname: Scrutton – volume: 572 start-page: 97 year: 2001 ident: 1027_CR10 publication-title: J Mol Struct (Theochem) doi: 10.1016/S0166-1280(01)00587-5 contributor: fullname: SS Erdem – volume: 39 start-page: 15258 year: 2000 ident: 1027_CR25 publication-title: Biochemistry doi: 10.1021/bi001957h contributor: fullname: RK Nandigama – volume: 17 start-page: 687 year: 2012 ident: 1027_CR13 publication-title: J Biol Inorg Chem doi: 10.1007/s00775-012-0888-x contributor: fullname: MZ Ertem – volume: 41 start-page: 14111 year: 2002 ident: 1027_CR33 publication-title: Biochemistry doi: 10.1021/bi020309q contributor: fullname: A Tilocca – volume: 98 start-page: 10089 year: 1994 ident: 1027_CR18 publication-title: J Phys Chem doi: 10.1021/j100091a024 contributor: fullname: K Kim – volume: 38 start-page: 13670 year: 1999 ident: 1027_CR24 publication-title: Biochemistry doi: 10.1021/bi990920y contributor: fullname: JR Miller – volume: 114 start-page: 721 year: 2007 ident: 1027_CR35 publication-title: J Neural Transm doi: 10.1007/s00702-007-0678-8 contributor: fullname: J Wang – volume: 105 start-page: 5739 year: 2008 ident: 1027_CR30 publication-title: Proc Natl Acad Sci doi: 10.1073/pnas.0710626105 contributor: fullname: SY Son – volume: 114 start-page: 693 year: 2007 ident: 1027_CR1 publication-title: J Neural Transm doi: 10.1007/s00702-007-0670-3 contributor: fullname: MA Akyüz – volume: 461–462 start-page: 1 year: 1999 ident: 1027_CR6 publication-title: J Mol Struct (Theochem) doi: 10.1016/S0166-1280(98)00475-8 contributor: fullname: S Dapprich – volume: 6 start-page: 1 year: 2011 ident: 1027_CR19 publication-title: PLoS ONE contributor: fullname: X Kong – start-page: 177 volume-title: Advances in electron transfer chemistry year: 1992 ident: 1027_CR29 contributor: fullname: RB Silverman – volume: 120 start-page: 215 year: 2008 ident: 1027_CR39 publication-title: Theor Chem Acc doi: 10.1007/s00214-007-0310-x contributor: fullname: Y Zhao – volume: 493 start-page: 13 year: 2010 ident: 1027_CR14 publication-title: Arch Biochem Biophys doi: 10.1016/j.abb.2009.07.019 contributor: fullname: PF Fitzpatrick – volume: 110 start-page: 13608 year: 2006 ident: 1027_CR26 publication-title: J Phys Chem B doi: 10.1021/jp0619181 contributor: fullname: R Prabhakar – volume: 33 start-page: 14871 year: 1994 ident: 1027_CR17 publication-title: Biochemistry doi: 10.1021/bi00253a026 contributor: fullname: T Jonsson – volume: 98–2 start-page: 1372 year: 1993 ident: 1027_CR2 publication-title: J Chem Phys doi: 10.1063/1.464304 contributor: fullname: AD Becke – ident: 1027_CR15 – volume: 118 start-page: 1021 year: 2011 ident: 1027_CR9 publication-title: J Neural Transm doi: 10.1007/s00702-011-0635-4 contributor: fullname: SS Erdem – volume: 393 start-page: 51 year: 2004 ident: 1027_CR37 publication-title: Chem Phys Lett doi: 10.1016/j.cplett.2004.06.011 contributor: fullname: T Yanai – volume: 11 start-page: 1983 year: 2004 ident: 1027_CR8 publication-title: Curr Med Chem doi: 10.2174/0929867043364784 contributor: fullname: DE Edmondson – volume: 11 start-page: 1228 year: 2010 ident: 1027_CR7 publication-title: Chem Bio Chem doi: 10.1002/cbic.201000184 contributor: fullname: RV Dunn – volume: 5 start-page: 1749 year: 2009 ident: 1027_CR28 publication-title: J Chem Theory Comput doi: 10.1021/ct9000922 contributor: fullname: J Rezac – volume: 100 start-page: 9750 year: 2003 ident: 1027_CR3 publication-title: Proc Natl Acad Sci doi: 10.1073/pnas.1633804100 contributor: fullname: C Binda – start-page: 817 volume-title: Flavins and flavoproteins year: 2002 ident: 1027_CR22 contributor: fullname: X Lu – volume: 34 start-page: 121 year: 2013 ident: 1027_CR38 publication-title: J Comput Chem doi: 10.1002/jcc.23112 contributor: fullname: L Yuan – volume: 10 start-page: 6615 year: 2008 ident: 1027_CR4 publication-title: Phys Chem Chem Phys doi: 10.1039/b810189b contributor: fullname: JD Chai – volume: 13 start-page: 1173 year: 2007 ident: 1027_CR32 publication-title: J Mol Model doi: 10.1007/s00894-007-0233-4 contributor: fullname: JJP Stewart – volume: 111 start-page: 10439 year: 2007 ident: 1027_CR31 publication-title: J Phys Chem A doi: 10.1021/jp0734474 contributor: fullname: SF Sousa – volume: 102 start-page: 12684 year: 2005 ident: 1027_CR5 publication-title: Proc Natl Acad Sci doi: 10.1073/pnas.0505975102 contributor: fullname: LD Colibus – volume: 4 start-page: 646 year: 2006 ident: 1027_CR11 publication-title: Org Biomol Chem doi: 10.1039/b511350d contributor: fullname: SS Erdem – volume: 133 start-page: 12319 year: 2011 ident: 1027_CR23 publication-title: J Am Chem Soc doi: 10.1021/ja205629b contributor: fullname: S MacMillar – ident: 1027_CR34 doi: 10.1002/ejoc.201201122 – year: 2013 ident: 1027_CR12 publication-title: J Enzyme Inhib Med Chem contributor: fullname: SS Erdem – volume: 37–2 start-page: 785 year: 1988 ident: 1027_CR20 publication-title: Phys Rev B doi: 10.1103/PhysRevB.37.785 contributor: fullname: C Lee – volume: 7 start-page: 1494 year: 2011 ident: 1027_CR21 publication-title: J Chem Theory Comput doi: 10.1021/ct200031t contributor: fullname: R-Z Liao – volume: 50 start-page: 7710 year: 2011 ident: 1027_CR36 publication-title: Biochemistry doi: 10.1021/bi200951z contributor: fullname: J Wang – volume: 46 start-page: 7655 year: 2007 ident: 1027_CR27 publication-title: Biochemistry doi: 10.1021/bi700482h contributor: fullname: EC Ralph |
| SSID | ssj0001178 ssj0053170 ssj0053176 |
| Score | 2.320244 |
| Snippet | Monoamine oxidases are two isozymic flavoenzymes which are the important targets for drugs used in the treatment of depression, Parkinson and Alzheimer’s... Monoamine oxidases are two isozymic flavoenzymes which are the important targets for drugs used in the treatment of depression, Parkinson and Alzheimer's... Issue Title: Special Issue: 15th Amine Oxidase Conference: Re-Examining Amines Monoamine oxidases are two isozymic flavoenzymes which are the important targets... |
| SourceID | proquest crossref pubmed springer |
| SourceType | Aggregation Database Index Database Publisher |
| StartPage | 937 |
| SubjectTerms | Animals Benzylamines - pharmacology Catalytic Domain Computer Simulation Humans Medicine Medicine & Public Health Models, Chemical Molecular Dynamics Simulation Monoamine Oxidase - chemistry Monoamine Oxidase - metabolism Neurology Neurosciences Oxidation-Reduction - drug effects Phenethylamines - pharmacology Psychiatry Translational Neurosciences - Original Article |
| Title | Computational modeling of the direct hydride transfer mechanism for the MAO catalyzed oxidation of phenethylamine and benzylamine: ONIOM (QM/QM) calculations |
| URI | https://link.springer.com/article/10.1007/s00702-013-1027-8 https://www.ncbi.nlm.nih.gov/pubmed/23619993 https://www.proquest.com/docview/1355329318 https://search.proquest.com/docview/1356391037 https://search.proquest.com/docview/1367493626 |
| Volume | 120 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV3ra9RAEB9qC-IX0dbHaS0jiPggmuym2azfUulZldxR8KB-CslmF4teTnpX8Pq_-L86s3moVAU_hWWHycLM7vx25wXwyNKlw0VOBspESRBrEwe61jIQqSN4nipbOc4dzifJ0Sx-d7J_sgFieLpoPr_oPZL-oB5y3bgwDUcRcCiVoJP1CmztczU00uGZyIbTN4rU4EYg_WJt_DloPZdhGNCtIO59nH9i_ruVugQ9L7lNvTUa34DrHYzErJX7TdiwzTbsZA1doedrfIw-sNO_mG_D1bzzn-_A97aJQ_cAiL4NDvHHhUMCgtjaN_y05p7rFlce1NoznFvODz5dzpEgrqfMsyn6l5_1ha1x8e20bc3EjDhozJL4SdXon1g2NVa2uejGr3A6eTvN8clx_vI4f0pMvpiug9jyFszGhx9eHwVdg4bAkE1bBTaSyqRauNBxnbQyJaxmlTVJbYQN68qYuIyrWFdSEcwpS12npaKJ2lWEVKyQt2GzWTT2LqDRUnKlVGNDE4dllFbaOJHIWjijpDEjeNYLpPja1uEohorLXnoFSa9g6RXpCHZ7kRXdllwWESErSeAmoumHwzRtJvaQlI1dnHsaQmycOvkvmkTFmqv4jOBOqw7DiriSDSFuOYLnvX78soC_Lffef1Hfh2uibclB-roLm6uzc_uAgNGq2oOtbHxwMOHvm4_vD_f8zvgBk6IFkw |
| link.rule.ids | 315,783,787,27936,27937,41093,41535,42162,42604,52123,52246 |
| linkProvider | Springer Nature |
| linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV1bb9MwFD6CTgJeBmwMCgOMhBAwZcQXkpi3Cm10bGk1qZPGU5Q4tphYU7SmEu1_4b9ybCfhMkDao2XLF53P9mefG8BzjY8OQw0PYkWjQEglAllKHrDEID1PYl0Y6zucjqLhifh4-va08eOet9burUrSndSds5uNTGPNCKwtFcOj9TqsCUYj1oO1wYdPh3vdAUxp3GkSEGIWkD8LXnkZhgE-DESr5vxb979fVJfY5yXNqbuQ9m_DpF2Kt0P5sruoi121-iPK4xXXegfWG4JKBh5Rd-GarjZgc1Dh43y6JC-IMxl1f_EbcCNtNPOb8N2nh2i-FolLsIMjkpkhSDGJvznJ56XN5q5J7eiyviBTbT2Pz-ZTguTZtUwHY-L-lJYrXZLZtzOf9Ml2ZM3RNAILQYxjkrwqSaGrVVN-R8ajg3FKXh6nb47TV9jJuWpyk83vwcn-3uT9MGhSPwQKb8s60JTHKpHMhMZGYMsTZIE61ioqFdNhWSglclEIWfAYCVSeyzLJY6woTYEcSDO-Bb1qVukHQJTk3MZgVTpUIsxpUkhlWMRLZlTMlerD61bO2Vcf4SPrYjk7OWQoh8zKIUv6sN0iIWs2-zyjyNk40iaK1c-6atymVveSV3q2cG2QC1qnzP-1iWIhbXygPtz3KOtmZGPkIJfnfdhpEfPLBP413YdXav0Ubg4n6VF2dDA6fAS3mE_8gSjchl59sdCPkX7VxZNmu_0AG28ilA |
| linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1bb9MwFD6CTpp44bJxKQwwEkLAlDWJTZzwVsHKxkjLJCaNpxDfxARNpzWVaP8L_5VjOwmXARLi0bLl2PIX-7PPOd8BeKjx0mEiQwMuoyRgmWRBpjIaxKlBep5yLYyNHc7Hyd4Re3387LjJczpvvd1bk6SPabAqTVU9OFVm0AW-WZUa61Jg_api3GYvwhqzwkg9WBu-en-w223GUcQ7qwLCzYLze8EbMsMwwEsCa02ev-v-50PrHBM9Z0V1h9PoCnxop-V9Uj7tLGqxI1e_KD7-x7yvwuWGuJKhR9o1uKCrDdgcVnhpny7JI-JcSd0b_Qas543FfhO--rQRzZMjcYl38OtkZghST-JPVPJxabO8a1I7Gq3PyFTbiOST-ZQgqXYt8-GEuLem5UorMvty4pNB2Y6sm5pGwCG48ZukrBQRulo15edkMt6f5OTxYT44zJ9gJ59lk7Nsfh2ORrvvXuwFTUqIQOIpWgc6olymWWxCY5XZyhTZoeZaJkrGOlRCSlYywTJBORKrssxUWnKsUEYgN9IxvQG9albpW0BkRqnVZpU6lCwso1Rk0sQJVbGRnErZh6ftmhenXvmj6DSe3ToUuA6FXYci7cNWi4qi2QTmRYRcjiKdirD6QVeNv6-1yZSVni1cG-SINljzb20SzjKrG9SHmx5x3Yisdg5yfNqH7RY9PwzgT8O9_U-t78P625ej4s3--OAOXIp9PhAE4Rb06rOFvousrBb3mj_vGz5SK3g |
| 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=Computational+modeling+of+the+direct+hydride+transfer+mechanism+for+the+MAO+catalyzed+oxidation+of+phenethylamine+and+benzylamine%3A+ONIOM+%28QM%2FQM%29+calculations&rft.jtitle=Journal+of+neural+transmission+%28Vienna%2C+Austria+%3A+1996%29&rft.au=Aky%C3%BCz%2C+Mehmet+Ali&rft.au=Erdem%2C+Safiye+Sa%C4%9F&rft.date=2013-06-01&rft.eissn=1435-1463&rft.volume=120&rft.issue=6&rft.spage=937&rft.epage=945&rft_id=info:doi/10.1007%2Fs00702-013-1027-8&rft.externalDBID=NO_FULL_TEXT |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0300-9564&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0300-9564&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0300-9564&client=summon |