F sub(420)H sub(2): Quinone oxidoreductase from Archaeoglobus fulgidus. Characterization of a membrane-bound multisubunit complex containing FAD and iron-sulfur clusters
Archaeoglobus fulgidus, a hyperthermophilic sulfate-reducing archaeon, was found to contain a membrane-bound F sub(420)H sub(2): quinone oxidoreductase complex presumed to be involved in energy conservation during growth on lactate plus sulfate. After solubilization with dodecyl- beta -D-maltoside t...
Saved in:
Published in | European journal of biochemistry Vol. 223; no. 2; pp. 503 - 511 |
---|---|
Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
01.01.1994
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Archaeoglobus fulgidus, a hyperthermophilic sulfate-reducing archaeon, was found to contain a membrane-bound F sub(420)H sub(2): quinone oxidoreductase complex presumed to be involved in energy conservation during growth on lactate plus sulfate. After solubilization with dodecyl- beta -D-maltoside the complex was purified 32-fold with a yield of 24%. Using both gel filtration and native PAGE, an apparent molecular mass of approximately 270 kDa was determined. SDS/PAGE revealed the presence of at least seven polypeptides with apparent molecular masses 56, 45, 41, 39, 37, 33, and 32 kDa. The purified complex contained 1.6 mol FAD, 9 mol non-heme iron and 7 mol acid-labile sulfur/mol complex. It did not contain cytochromes, which were, however, present in the membrane fraction of A. fulgidus (3 nmol/mg membrane protein). The purified F sub(420)H sub(2):quinone oxidoreductase complex catalyzed the reduction of 2,3-dimethyl-1,4-naphthoquinone (apparent K sub(m) 190 mu M) with reduced coenzyme F sub(420) (apparent K sub(m) 50 mu M) exhibiting a specific activity of 500 U/mg (apparent V sub(max)) at pH 8.0 (pH optimum) and 65 degree C (temperature optimum). 2-Methyl-1,4-naphthoquinone (menadione), 2-hydroxy-1,4-naphthoquinone, 1,4-naphthoquinone, 2,3-dimethoxy-5-methyl-1,4-benzoquinone, and 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone (decyl-ubiquinone) were also reduced with F sub(420)H sub(2), albeit with lower rates. The physiological electron acceptor of the F sub(420)H sub(2):quinone oxidoreductase complex is most likely the menaquinone found in the membrane fraction of A. fulgidus. |
---|---|
AbstractList | Archaeoglobus fulgidus, a hyperthermophilic sulfate-reducing archaeon, was found to contain a membrane-bound F sub(420)H sub(2): quinone oxidoreductase complex presumed to be involved in energy conservation during growth on lactate plus sulfate. After solubilization with dodecyl- beta -D-maltoside the complex was purified 32-fold with a yield of 24%. Using both gel filtration and native PAGE, an apparent molecular mass of approximately 270 kDa was determined. SDS/PAGE revealed the presence of at least seven polypeptides with apparent molecular masses 56, 45, 41, 39, 37, 33, and 32 kDa. The purified complex contained 1.6 mol FAD, 9 mol non-heme iron and 7 mol acid-labile sulfur/mol complex. It did not contain cytochromes, which were, however, present in the membrane fraction of A. fulgidus (3 nmol/mg membrane protein). The purified F sub(420)H sub(2):quinone oxidoreductase complex catalyzed the reduction of 2,3-dimethyl-1,4-naphthoquinone (apparent K sub(m) 190 mu M) with reduced coenzyme F sub(420) (apparent K sub(m) 50 mu M) exhibiting a specific activity of 500 U/mg (apparent V sub(max)) at pH 8.0 (pH optimum) and 65 degree C (temperature optimum). 2-Methyl-1,4-naphthoquinone (menadione), 2-hydroxy-1,4-naphthoquinone, 1,4-naphthoquinone, 2,3-dimethoxy-5-methyl-1,4-benzoquinone, and 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone (decyl-ubiquinone) were also reduced with F sub(420)H sub(2), albeit with lower rates. The physiological electron acceptor of the F sub(420)H sub(2):quinone oxidoreductase complex is most likely the menaquinone found in the membrane fraction of A. fulgidus. |
Author | Linder, D Kunow, J Stetter, KO Thauer, R K |
Author_xml | – sequence: 1 givenname: J surname: Kunow fullname: Kunow, J – sequence: 2 givenname: D surname: Linder fullname: Linder, D – sequence: 3 givenname: KO surname: Stetter fullname: Stetter, KO – sequence: 4 givenname: R surname: Thauer middlename: K fullname: Thauer, R K |
BookMark | eNqNjUFOwzAQRb0oEi1wh1khughyQ3EUdlWh6haJfeU4k9TI9hSPR6q4EbckIA7A6v3F__8t1CxRwpmaa71aV3X7aC7Vgvlda21a08zV1w5Yurt1rZf731Qvn-BV_M8M6Ox7ytiLK5YRhkwRNtkdLdIYqBOGQcLoe-F72B5ttq5g9p-2eEpAA1iIGLtsE1YdSeohSih-skjyBRzFU8DzxFSsTz6NsNs8g516PlOqWMIgGVwQnm75Wl0MNjDe_PFK3e5e3rb76pTpQ5DLIXp2GMKkI-HDypim1Y15-HfxG0R5Y-o |
ContentType | Journal Article |
DBID | 7QL C1K F1W H95 L.G |
DatabaseName | Bacteriology Abstracts (Microbiology B) Environmental Sciences and Pollution Management ASFA: Aquatic Sciences and Fisheries Abstracts Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources Aquatic Science & Fisheries Abstracts (ASFA) Professional |
DatabaseTitle | Aquatic Science & Fisheries Abstracts (ASFA) Professional Bacteriology Abstracts (Microbiology B) ASFA: Aquatic Sciences and Fisheries Abstracts Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources Environmental Sciences and Pollution Management |
DatabaseTitleList | Aquatic Science & Fisheries Abstracts (ASFA) Professional |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Chemistry Anatomy & Physiology |
EndPage | 511 |
GroupedDBID | -DZ -~X .55 .GJ 1OC 24P 36B 3O- 4.4 51W 51X 52N 52O 52P 52R 52T 52W 52X 53G 5GY 5HH 5LA 5RE 66C 7PT 7QL 8-1 AAZKR ABDBF ABEFU ABJNI ACGFS ACNCT ACXQS ADBBV AETEA AEUQT AFBPY AI. ALMA_UNASSIGNED_HOLDINGS AMBMR BAWUL BY8 C1K CAG COF CS3 D-7 D-F DIK E3Z EAD EAP EAS EAU EBB EBC EBD EBS EBX EJD EMB EMK EMOBN EST ESX F04 F1W F5P GODZA GX1 H95 IH2 L.G L7B LW6 MVM O9- P4D RIG SUPJJ SV3 TR2 TUS VH1 WH7 WXI X7M Y6R YSK ZGI |
ID | FETCH-proquest_miscellaneous_166790763 |
ISSN | 0014-2956 |
IngestDate | Fri Aug 16 10:06:45 EDT 2024 |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 2 |
Language | English |
LinkModel | OpenURL |
MergedId | FETCHMERGED-proquest_miscellaneous_166790763 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 content type line 23 ObjectType-Feature-2 |
PQID | 16679076 |
PQPubID | 23462 |
ParticipantIDs | proquest_miscellaneous_16679076 |
PublicationCentury | 1900 |
PublicationDate | 19940101 |
PublicationDateYYYYMMDD | 1994-01-01 |
PublicationDate_xml | – month: 01 year: 1994 text: 19940101 day: 01 |
PublicationDecade | 1990 |
PublicationTitle | European journal of biochemistry |
PublicationYear | 1994 |
SSID | ssj0006967 |
Score | 2.7225385 |
Snippet | Archaeoglobus fulgidus, a hyperthermophilic sulfate-reducing archaeon, was found to contain a membrane-bound F sub(420)H sub(2): quinone oxidoreductase complex... |
SourceID | proquest |
SourceType | Aggregation Database |
StartPage | 503 |
SubjectTerms | Archaeoglobus fulgidus Freshwater |
Title | F sub(420)H sub(2): Quinone oxidoreductase from Archaeoglobus fulgidus. Characterization of a membrane-bound multisubunit complex containing FAD and iron-sulfur clusters |
URI | https://search.proquest.com/docview/16679076 |
Volume | 223 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1bS-tAEF6qL_pyOOoRjx51HkSUEEm2SWx8K2oo4uUIFfpWss1GCjWBJgvqPzr_8sxemqRe8PISNiFs2p2PmZ2dmW8I2QvRbrBOzGzWSRMb_Q1us_bxyPbihDuJ6ya-Ip6_ug56d97FwB-0Wk-NrCVRsqPR85t1Jd-RKj5Ducoq2S9ItpoUH-AY5YtXlDBePyXjyCoEwy2iRx306HvmjuJYOvq3Yoy-Pbfyx7FsJyKJXdFk6YISSTgb81zSgYjCSsXkfpyI4khF3zV_83O1l5Rtph_Qqc5wgWUTJp2EiN8SqA50Tjp_VDnvutuEFXXPdEximmd2ISapmFqjiZCUDMW7kQCzK2Zj2cJL96Crw0yZjkBVZ9ryJEFjrU5YLlVhklJcN3W6SyxMc2dznpuYij-vccBhlLbr2TTU_OMzpU11lbJBJ22oYN9pN6y5b1T5HNH29c0wuru8HPbPB_0FstB2ZS4o9f5WJjwIA022ar78ylCr3Uf_J_lh3AboagyskBbPVslaN4vL_OEJ9kEl8qoIySpZOp0t4Br5FwEK6gABcthTI3p4AgYYMA8MkMCAOWBABQx4CQzIU4hhHhjQBAYYYEANDEBgAAIDGsCAGTB-kf3ovH_as2dLMMT_IMNKOH0uiqEbBMehg3ZqnSzKX79BIPWYT502cxOUZ0h5LDmf0o7rsE7APR7_JrsfTLb54RtbZLlGyx-yWE4F38YNYsl2lDD_A0kveQY |
link.rule.ids | 315,786,790 |
linkProvider | Wiley-Blackwell |
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=F+sub%28420%29H+sub%282%29%3A+Quinone+oxidoreductase+from+Archaeoglobus+fulgidus.+Characterization+of+a+membrane-bound+multisubunit+complex+containing+FAD+and+iron-sulfur+clusters&rft.jtitle=European+journal+of+biochemistry&rft.au=Kunow%2C+J&rft.au=Linder%2C+D&rft.au=Stetter%2C+KO&rft.au=Thauer%2C+R+K&rft.date=1994-01-01&rft.issn=0014-2956&rft.volume=223&rft.issue=2&rft.spage=503&rft.epage=511&rft.externalDBID=NO_FULL_TEXT |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0014-2956&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0014-2956&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0014-2956&client=summon |