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The respiratory supercomplex factor 1 (Rcf 1) in  Saccharomyces cerevisiae  binds to intact cytochrome  c  oxidase (Cyt c O) and has also been suggested to be an assembly factor of the enzyme. Here, we isolated Cyt c O from  rcf1 Δ mitochondria using affinity chromatography and investigated reduction, inter-heme electron transfer and ligand binding to heme  a  3 . The data show that removal of Rcf1 yields two Cyt c O sub-populations. One of these sub-populations exhibits the same functional behavior as Cyt c O isolated from the wild-type strain, which indicates that intact Cyt c O is assembled also without Rcf1. In the other sub-population, which was shown previously to display decreased activity and accelerated ligand-binding kinetics, the midpoint potential of the catalytic site was lowered. The lower midpoint potential allowed us to selectively reduce one of the two sub-populations of the  rcf1 Δ Cyt c O, which made it possible to investigate the functional behavior of the two Cyt c O forms separately. We speculate that these functional alterations reflect a mechanism that regulates O 2  binding and trapping in Cyt c O, thereby altering energy conservation by the enzyme.

Regulation of cytochrome c oxidase activity by modulation of the catalytic site