The kinetics of electron entry in cytochromec oxidase
- 1 January 1990
- journal article
- research article
- Published by Springer Nature in BioMetals
- Vol. 3 (2) , 118-121
- https://doi.org/10.1007/bf01179517
Abstract
The kinetics of electron entry in beef heart cytochromec oxidase have been studied by stopped-flow spectroscopy following chemical modification of the CuA site with mercurials. In this derivative CuA is no longer reducible by cytochrome c while cytochromea may accept electrons from the latter with rates comparable to the native enzyme. The results indicate that CuA is not the exclusive electron entry site in cytochromec oxidase.Keywords
This publication has 15 references indexed in Scilit:
- The mechanism of proton translocation in respiration and photosynthesisFEBS Letters, 1989
- Extended x-ray absorption fine structure of copper in CuA-depleted, p-(hydroxymercuri)benzoate-modified, and native cytochrome c oxidaseBiochemistry, 1987
- Cytochrome oxidase: a perspectivePublished by Walter de Gruyter GmbH ,1987
- Influence of detergent polar and apolar structure upon the temperature dependence of beef heart cytochrome c oxidase activityBiochemistry, 1985
- Chemical modification of the copperA center in cytochrome c oxidase by sodium p-(hydroxymercuri)benzoateBiochemistry, 1985
- Studies on partially reduced mammalian cytochrome oxidase reactions with ferrocytochrome cBiochemical Journal, 1976
- Characterization of the Reaction between Ferrocytochrome c and Cytochrome c OxidaseEuropean Journal of Biochemistry, 1975
- Structural implications derived from the analysis of electron paramagnetic resonance spectra of natural and artificial copper proteinsArchives of Biochemistry and Biophysics, 1974
- The reaction of ferrocytochrome c with cytochrome oxidase: A new lookFEBS Letters, 1972
- Determination of heme a concentration in cytochrome preparations by hemochromogen methodAnalytical Biochemistry, 1965