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
相关论文
共 34 条
[21]   Distinct constitutive and low-CO2-induced CO2 uptake systems in cyanobacteria:: Genes involved and their phylogenetic relationship with homologous genes in other organisms [J].
Shibata, M ;
Ohkawa, H ;
Kaneko, T ;
Fukuzawa, H ;
Tabata, S ;
Kaplan, A ;
Ogawa, T .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (20) :11789-11794
[22]   Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp APS [J].
Shigenobu, S ;
Watanabe, H ;
Hattori, M ;
Sakaki, Y ;
Ishikawa, H .
NATURE, 2000, 407 (6800) :81-86
[23]  
Singer T P, 1979, Methods Enzymol, V55, P454
[24]   Overexpression of the Escherichia coli nuo-operon and isolation of the overproduced NADH:ubiquinone oxidoreductase (Complex I) [J].
Spehr, V ;
Schlitt, A ;
Scheide, D ;
Guénebaut, V ;
Friedrich, T .
BIOCHEMISTRY, 1999, 38 (49) :16261-16267
[25]   Extremophiles and their adaptation to hot environments [J].
Stetter, KO .
FEBS LETTERS, 1999, 452 (1-2) :22-25
[26]   A genomic perspective on protein families [J].
Tatusov, RL ;
Koonin, EV ;
Lipman, DJ .
SCIENCE, 1997, 278 (5338) :631-637
[27]   The COG database: new developments in phylogenetic classification of proteins from complete genomes [J].
Tatusov, RL ;
Natale, DA ;
Garkavtsev, IV ;
Tatusova, TA ;
Shankavaram, UT ;
Rao, BS ;
Kiryutin, B ;
Galperin, MY ;
Fedorova, ND ;
Koonin, EV .
NUCLEIC ACIDS RESEARCH, 2001, 29 (01) :22-28
[28]   Alternative respiratory pathways of Escherichia coli: Energetics and transcriptional regulation in response to electron acceptors [J].
Unden, G ;
Bongaerts, J .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 1997, 1320 (03) :217-234
[29]   THE NADH - UBIQUINONE OXIDOREDUCTASE (COMPLEX-I) OF RESPIRATORY CHAINS [J].
WALKER, JE .
QUARTERLY REVIEWS OF BIOPHYSICS, 1992, 25 (03) :253-324
[30]   THE RESPIRATORY-CHAIN NADH DEHYDROGENASE (COMPLEX-I) OF MITOCHONDRIA [J].
WEISS, H ;
FRIEDRICH, T ;
HOFHAUS, G ;
PREIS, D .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1991, 197 (03) :563-576