Cytochrome oxidase: an alternative model.
Oxidative titration of reduced cytochrome oxidase (cytochrome c oxidase; ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1) in the presence of carbon monoxide and sulfide, at potentials greater than +500 mV (vs. the neutral hydrogen electrode), have failed to produce new copper signals in the electron paramagnetic resonance spectrum of this enzyme. This observation implies that once of the copper centers in cytochrome oxidase remains Cu(I) under strongly oxidizing conditions. The rationalization of this fact, and the possible explanation of a great accumulation of spectroscopic data, is that cytochrome a3 may be a two-electron redox center, with stable Fe(IV), Fe(III), and Fe(II) states during its redox cycle. This oxidase model does not require an antiferromagnetic coupling scheme, in contrast to currently prevalent models.
D000818:Animals; D002248:Carbon Monoxide; D002417:Cattle; D003300:Copper; D004578:Electron Spin Resonance Spectroscopy; D003576:Electron Transport Complex IV; D008929:Mitochondria, Heart / Q000201:enzymology; D010084:Oxidation-Reduction; D011487:Protein Conformation; D013059:Spectrum Analysis, Raman
D003300:Copper; D002248:Carbon Monoxide; D003576:Electron Transport Complex IV