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

Gary Cecchini, Elena Maklashina, Victoria Yankovskaya, Tina M Iverson, So Iwata

Journal: FEBS letters 2003;545(1):31-8

PMID: 12788489

Abstract

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.

Address: Molecular Biology Division (151-S), VA Medical Center and Department of Biochemistry and Biophysics, University of California, San Francisco, CA, USA. [email protected]

DOI: 10.1016/s0014-5793(03)00390-9

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MeSH Terms: Benzoquinones, Binding Sites, Catalysis, Electron Transport, Electron Transport Complex II, Escherichia coli, Ion Transport, Models, Molecular, Multienzyme Complexes, Oxidoreductases, Protons, Succinate Dehydrogenase