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

doi:10.1021/bi961488c

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Article

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

Biochemistry - 10 Dec 1996

Miller M A

Abstract excerpt

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 approxi...

Topics

Binding Sites
Cytochrome c Group
Cytochrome-c Peroxidase
Electron Transport
Fungal Proteins
Hydrogen Peroxide
Kinetics
Models, Chemical
Models, Molecular
Mutation
Osmolar Concentration
Oxidation-Reduction
Recombinant Proteins
Yeasts

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