An Escherichia coli mutant quinol:fumarate reductase contains an EPR-detectable semiquinone stabilized at the proximal quinone-binding site

The EPR and thermodynamic properties of semiquinone (SQ) species stabilized by mammalian succinate:quinone reductase (SQR) in situ in the mitochondrial membrane and in the isolated enzyme have been well documented. The equivalent semiquinones in bacterial membranes have not yet been characterized, e...

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Vydáno v:	The Journal of biological chemistry Ročník 274; číslo 37; s. 26157
Hlavní autoři:	Hägerhäll, C, Magnitsky, S, Sled, V D, Schröder, I, Gunsalus, R P, Cecchini, G, Ohnishi, T
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	United States 10.09.1999
Témata:	Binding Sites Electron Spin Resonance Spectroscopy Electron Transport Complex II Escherichia coli - genetics Multienzyme Complexes - chemistry Multienzyme Complexes - genetics Multienzyme Complexes - metabolism Mutation Oxidoreductases - chemistry Oxidoreductases - genetics Oxidoreductases - metabolism Quinones - metabolism Succinate Dehydrogenase - chemistry Succinate Dehydrogenase - genetics Succinate Dehydrogenase - metabolism
ISSN:	0021-9258
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