Kinetics of cytochrome c oxidase from yeast. Membrane-facilitated electrostatic binding of cytochrome c showing a specific interaction with cytochrome c oxidase and inhibition by ATP (With an appendix on the occurrence of two-dimensional diffusion of cytochrome c on the membrane surface)
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference95 articles.
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1. The Number of Nucleotide Binding Sites in Cytochrome C Oxidase;Biochemical and Biophysical Research Communications;1995-12
2. Disproportionate regulation of nuclear- and mitochondrial-encoded cytochrome oxidase subunit proteins by functional activity in neurons;Neuroscience;1995-07
3. Regulation of Cytochrome c Oxidase by Interaction of ATP at Two Binding Sites, One on Subunit VIa;Biochemistry;1994-10-04
4. Comparison of Electron Transfer Kinetics between Redox Proteins Free in Solution and Electrostatically Complexed to a Lipid Bilayer Membrane;Archives of Biochemistry and Biophysics;1994-05
5. Subunit VIa of yeast cytochrome c oxidase is not necessary for assembly of the enzyme complex but modulates the enzyme activity. Isolation and characterization of the nuclear-coded gene.;Journal of Biological Chemistry;1993-09
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