Abstract
Reduction of detergent-solubilized formate-inhibited beef heart cytochrome c oxidase +/- cytochrome c in turnover with ascorbate was followed aerobically. Heme c, heme a and CuA steady states were monitored. Heme a and CuA were in equilibrium with each other, and with cytochrome c when the latter was present. In the formate system there is no aerobic reduction of any binuclear centre component (heme a3 or CuB). At pH 7.4 and 30 deg C calculated E0’values were +310 mV for heme a and +260 mV for CuA, assuming E0’for cyt.
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