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J. Biol. Chem., Vol. 262, Issue 12, 5441-5444, 04, 1987
S Japa, QS Zhu and DS Beattie
The functional role and topographical orientation in the inner membrane of
subunit VII, the ubiquinone-binding protein, of the cytochrome b-c1 complex
of yeast mitochondria has been investigated. The apparent molecular weight
of this subunit on sodium dodecyl sulfate-urea gels was calculated to be
15,500, while its amino acid composition was similar to that of the
Q-binding proteins present in the cytochrome b- c1 complexes isolated from
both beef heart and yeast mitochondria. The specific antibody obtained
against subunit VII inhibited 30-47% of the ubiquinol-cytochrome c
reductase activity in the isolated cytochrome b- c1 complex and in
submitochondrial particles but had no effect on cytochrome c reductase
activity in mitoplasts, mitochondria from which the outer membrane has been
removed. Furthermore, the antibody against subunit VII strongly inhibited
(74%) the reduction of cytochrome b by succinate in the presence of
antimycin, an inhibitor of center i, but had no effect on cytochrome b
reduction in the presence of myxothiazol, an inhibitor of center o. These
results suggest that subunit VII, the Q- binding protein, is involved in
electron transport at center o of the cytochrome b-c1 complex of the
respiratory chain and that subunit VII is localized facing the matrix side
of the inner mitochondrial membrane.
Subunit VII, the ubiquinone-binding protein, of the cytochrome b-c1 complex of yeast mitochondria is involved in electron transport at center o and faces the matrix side of the membrane
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