Article
Fumarate reductase and succinate oxidase activity of Escherichia coli complex II homologs are perturbed differently by mutation of the flavin binding domain.
The Journal of biological chemistry - 21 Apr 2006
Maklashina Elena, Iverson Tina M, Sher Yelizaveta, Kotlyar Violetta, Andréll Juni, Mirza Osman, Hudson Janette M, Armstrong Fraser A, Rothery Richard A, Weiner Joel H, Cecchini Gary
Abstract excerpt
The Escherichia coli complex II homologues succinate:ubiquinone oxidoreductase (SQR, SdhCDAB) and menaquinol:fumarate oxidoreductase (QFR, FrdABCD) have remarkable structural homology at their dicarboxylate binding sites. Although both SQR and QFR can catalyze the interconversion of fumarate and succinate, QFR is a much better fumarate reductase, and SQR is a better succinate oxidase. An exception to the...
Topics
- Alanine
- Amino Acids
- Binding Sites
- Catalysis
- Electrochemistry
- Electron Spin Resonance Spectroscopy
- Electron Transport Complex IV
- Electrons
- Enzyme Activation