A complete mechanism for steady-state oxidation of yeast cytochrome c by yeast cytochrome c peroxidase

Biochemistry
M A Miller

Abstract

Steady-state oxidation of yeast cytochrome c (yCc) was monitored as a function of ionic strength (mu) for mutants of a cloned cytochrome c peroxidase [CcP(MI)]. The data are best interpreted in the context of a two binding site model, where the affinity of the two sites for yCc differs by approximately 1000-fold and rapid intracomplex electron transfer (ET) occurs only at the high-affinity site identified in the crystal structure. At low mu, catalysis is apparently limited by the rate of yCc dissociation from the reactive high-affinity site (koff). Binding of yCc at the low-affinity site increases koff and therefore increases the rate of catalysis. Mutations at the high-affinity site also increase the rate of catalysis by the 1:1 CcP(MI):yCc complex by increasing koff. Mutations at residues that interact strongly with yCc at the high-affinity site (Asp 34, Glu 290, and Ala 193) cause the greatest increase in koff (25-38-fold at mu = 20 mM). Mutations at residues that interact less strongly with yCc (Glu 32 and Glu 291) cause smaller increases in koff (10- and 3-fold, respectively, at mu = 20 mM). The results provide additional evidence that the high-affinity site formed in solution is similar to the one identified in the crysta...Continue Reading

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Citations

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