Variation in proton donor/acceptor pathways in succinate:quinone oxidoreductases

FEBS Letters

Cecchini, Gary¹  Iverson, Tina M²  Maklashina, Elena¹  Iwata, So²  Yankovskaya, Victoria¹ 

[1] Molecular Biology Division (151-S), VA Medical Center, 4150 Clement Street, San Francisco, CA 94121, USA;Department of Biological Sciences, Imperial College, London SW7 2AZ, UK

关键词: Succinate dehydrogenase;    Fumarate reductase;    Quinone oxidoreductase;    Complex II;    Electron transport;    Proton;    DNP-19;    2-[1-p-chlorophenyl)ethyl]-4;    6-dinitrophenol;    HQNO;    2-n-heptyl-4-hydroxyquinoline-N-oxide;    MQ;    menaquinone;    QD;    quinone distal binding site;    QP;    quinone proximal binding site;    QFR;    quinol:fumarate oxidoreductase;    SQR;    succinate:quinone oxidoreductase;    UQ;    ubiquinone;   

DOI  :  10.1016/S0014-5793(03)00390-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The anaerobically expressed fumarate reductase and aerobically expressed succinate dehydrogenase from Escherichia coli comprise two different classes of succinate:quinone oxidoreductases (SQR), often termed respiratory complex II. The X-ray structures of both membrane-bound complexes have revealed that while the catalytic/soluble domains are structurally similar the quinone binding domains of the enzyme complexes are significantly different. These results suggest that the anaerobic and aerobic forms of complex II have evolved different mechanisms for electron and proton transfer in their respective membrane domains.

【 授权许可】

Unknown