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JBC, Vol. 253, Issue 7, 2392-2399, Apr, 1978
J. N. Siedow, S. Power, F. F. de la Rosa and G. Palmer
A soluble enzymically active cytochrome b.c1 complex has been purified from
baker's yeast mitochondria by a procedure involving solubilization in
cholate, differential fractionation with ammonium sulfate, and
ultracentrifugation. The resulting particle is free of both cytochrome c
oxidase and succinate dehydrogenase activities. The complex contains
cytochromes b and c1 in a ratio of 2:1 and quinone and iron-sulfur protein
in amounts roughly stoichiometric with cytochrome c1. EPR spectroscopy has
shown the iron-sulfur protein to be present mainly as the Rieske protein.
EPR spectroscopy also shows a heterogeneity in the cytochrome b population
with resonances appearing at g = 3.60 (cytochrome bK) and g = 3.76
(cytochrome bT). A third EPR resonance appearing in the region associated
with low spin ferric hemes (g = 3.49) is assigned to cytochrome c1.
Anaerobic titration of the complex with dithionite confirmed the
heterogeneity in the cytochrome b population and demonstrated that the
oxidation-reduction potential of the iron-sulfur protein is approximately
30 mV more positive than cytochrome c1. An intense EPR signal assigned to
the coenzyme Q free radical appeared midway in the reductive titration;
this signal disappeared toward the end of the titration. A conformational
change in the iron-sulfur protein attendant on reduction of a low potential
species was noted.
The preparation and characterization of highly purified, enzymically active complex III from baker's yeast
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