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The properties of the mitochondrial succinate-cytochrome c reductase

Authors :
Michele Koppelman
Maria Erecińska
John S. Leigh
David F. Wilson
Source :
Archives of Biochemistry and Biophysics. 151:112-121
Publication Year :
1972
Publisher :
Elsevier BV, 1972.

Abstract

The cytochromes b and b T of pigeon heart mitochondria have half-reduction potentials ( Em 's) of +30 mV and −30 mV at pH 7.2. The midpoint potentials of these cytochromes become more negative by 30–60 mV per pH unit when the pH is made more alkaline. Detergents may be used to prepare a succinate-cytochrome c reductase free of cytochrome oxidase in which the activation of electron transport induced by oxidation of cytochrome c 1 causes the half-reduction potential of cytochrome b T to become at least 175 mV more positive than in the absence of electron transport. This change is interpreted as indicating that the primary energy conservation reaction at site 2 remains fully functional in the purified reductase. Preliminary electron paramagnetic resonance spectra of the succinate-cytochrome c reductase as measured at near liquid helium temperatures are presented.

Details

ISSN :
00039861
Volume :
151
Database :
OpenAIRE
Journal :
Archives of Biochemistry and Biophysics
Accession number :
edsair.doi.dedup.....8e08e6c76dc7b7da3a46228756ba18be
Full Text :
https://doi.org/10.1016/0003-9861(72)90479-1