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. 1973 Sep;70(9):2477–2481. doi: 10.1073/pnas.70.9.2477

Electron Carriers of Cytochrome Oxidase Detectable by Electron Paramagnetic Resonance and Their Relationship to Those Traditionally Recognized in This Enzyme

Charles R Hartzell *, Raymond E Hansen †, Helmut Beinert †
PMCID: PMC427037  PMID: 4354851

Abstract

On the basis of oxidoreductive rapid kinetic and titration experiments with purified cytochrome c oxidase (EC 1.9.3.1), monitored by electron paramagnetic resonance (EPR) at 13°K and by spectrophotometry at 100°K, a new assignment of EPR signals is proposed. The bulk of both the low-spin (g = 3.0; 2.2; 1.5) and highspin (g = 6; 2) signals is attributed to the component with the properties of traditional cytochrome a. It is further proposed that the absorption band at 655 nm represents the most unambiguous manifestation of the a3 component.

Keywords: cytochrome a, a3; low-temperature spectra; rapid kinetics; redox titrations

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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