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Variation in proton donor/acceptor pathways in succinate:quinone oxidoreductases
Author(s) -
Cecchini Gary,
Maklashina Elena,
Yankovskaya Victoria,
Iverson Tina M,
Iwata So
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00390-9
Subject(s) - fumarate reductase , succinate dehydrogenase , quinone , escherichia coli , electron acceptor , enzyme , electron transport chain , chemistry , biochemistry , reductase , respiratory chain , electron transfer , membrane , electron transport complex i , stereochemistry , photochemistry , gene
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.