The proton-pumping NADH:ubiquinone oxidoreductase (complex 1) of Aquifex aeolicus

被引:20
作者
Scheide, D
Huber, R
Friedrich, T
机构
[1] Univ Dusseldorf, Inst Biochem, D-40225 Dusseldorf, Germany
[2] Univ Regensburg, Lehrstuhl Mikrobiol, D-93044 Regensburg, Germany
关键词
complex I; NADH : ubiquinone oxidoreductase; NADH dehydrogenase; extremophile; hyperthermophile; Aquifex aeolicus;
D O I
10.1016/S0014-5793(02)02224-X
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
The proton-pumping NADH:ubiquinone oxidoreductase, also called complex 1, is the first energy-transducing complex of many respiratory chains. Homologues of complex I are present in the three domains of life. Here. we report the properties of complex I in membranes of the hyperthermophilic bacterium Aquifex aeolicus. The complex reacted with NADH but not with NADPH and F420H2 as electron donors. Short-chain analogues of ubiquinone like decyl-ubiquinone and ubiquinone-2 were suitable electron acceptors. The affinities towards NADH and ubiquinone-2 were comparable to the ones obtained with the Escherichia coli complex I. The reaction was inhibited by piericidin A at the same concentration as in E. coli. The complex showed an unusual pH optimum at pH 9 and a maximal rate at 80degreesC. We found no evidence for the presence of an alternative. single subunit NADH dehydrogenase in A. aeolicus membranes. The NADH:ferricyanide reductase activity of detergent extracts of A. aeolicus membranes sedimented as a protein with a molecular mass of approximately 550 kDa. From the data Ne concluded that A. acolicus contains a NADH: ubiquinone oxidoreductase resembling complex I of mesophilic bacteria. (C) 2002 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:80 / 84
页数:5
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