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Escherichia coli Succinate Dehydrogenase Variant Lacking the Heme b
Quang M. Tran, Richard A. Rothery, Elena Maklashina, Gary Cecchini and Joel H. Weiner
Proceedings of the National Academy of Sciences of the United States of America
Vol. 104, No. 46 (Nov. 13, 2007), pp. 18007-18012
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/25450364
Page Count: 6
You can always find the topics here!Topics: Enzymes, P branes, Detergents, Signals, Ligands, Reactive oxygen species, Electron transfer, Absorption spectra, Quinones, Oxidation
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The Escherichia coli enzyme succinate:ubiquinone oxidoreductase [(succinate dehydrogenase (SdhCDAB)] couples succinate oxidation to ubiquinone reduction and is structurally and functionally equivalent to mitochondrial complex II, an essential component of the aerobic respiratory chain and tricarboxylic acid cycle. All such enzymes contain a heme within their membrane anchor domain with a highly contentious, but as-yet-undetermined, function. Here, we report the generation of a complex II that lacks heme, which is confirmed by both optical and EPR spectroscopy. Despite the absence of heme, this mutant still assembles properly and retains physiological activity. However, the mutants lacking heme are highly sensitive to the presence of detergent. In addition, the heme does not appear to be involved in reactive oxygen species suppression. Our results indicate that redox cycling of the heme in complex II is not essential for the enzyme's ubiquinol reductase activity.
Proceedings of the National Academy of Sciences of the United States of America © 2007 National Academy of Sciences