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Variation in proton donor/acceptor pathways in succinate:quinone oxidoreductases
Authors:Cecchini Gary  Maklashina Elena  Yankovskaya Victoria  Iverson Tina M  Iwata So
Affiliation:Molecular Biology Division (151-S), VA Medical Center and Department of Biochemistry and Biophysics, University of California, San Francisco, CA, USA. ceccini@itsa.ucsf.edu
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.
Keywords:Succinate dehydrogenase   Fumarate reductase   Quinone oxidoreductase   Complex II   Electron transport   Proton
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