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Progress in understanding structure–function relationships in respiratory chain complex II
Author(s) -
Ackrell Brian A.C
Publication year - 2000
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(99)01749-4
Subject(s) - electron transport chain , oxidoreductase , quinone , catalytic cycle , electron transport complex i , citric acid cycle , catalysis , respiratory chain , chemistry , fumarate reductase , function (biology) , protein structure , biochemistry , combinatorial chemistry , stereochemistry , enzyme , biology , succinate dehydrogenase , microbiology and biotechnology
Complex II (succinate:quinone oxidoreductase) of aerobic respiratory chains oxidizes succinate to fumarate and passes the electrons directly into the quinone pool. It serves as the only direct link between activity in the citric acid cycle and electron transport in the membrane. Finer details of these reactions and interactions are but poorly understood. However, complex II has extremely similar structural and catalytic properties to quinol:fumarate oxidoreductases of anaerobic organisms, for which X‐ray structures have recently become available. These offer new insights into structure–function relationships of this class of flavoenzymes, including evidence favoring protein movement during catalysis.