Learning from hydrogenases: location of a proton pump and of a second FMN in bovine NADH-ubiquinone oxidoreductase (Complex I)

被引:72
作者
Albracht, SPJ
Hedderich, R
机构
[1] Univ Amsterdam, Swammerdam Inst Life Sci, NL-1018 TV Amsterdam, Netherlands
[2] Max Planck Inst Terr Mikrobiol, D-35043 Marburg, Germany
关键词
NiFe]-hydrogenase; NADH-ubiquinone oxidoreductase; Complex I; proton pump; FMN;
D O I
10.1016/S0014-5793(00)02172-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Hydrogenases have clear evolutionary links to the much more complex NADH-ubiquinone oxidoreductases (Complex I). Certain membrane-bound [NiFe]-hydrogenases presumably pump protons. From a detailed comparison of hydrogenases and Complex I, it is concluded here that the TYKY subunit in these enzymes is a special 2[4Fe-4S] ferredoxin, which functions as the electrical driving unit for a proton pump. The comparison further revealed that the flavodoxin fold from [NiFe]-hydrogenases is presumably conserved in the PSST subunit of Complex I. It is proposed that bovine Complex I and the soluble NAD(+)-reducing hydrogenase from Ralstonia entropha each contain a second FMN group. (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
引用
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页码:1 / 6
页数:6
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