Interactions in cytochrome oxidase: Functions and structure |
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Authors: | Jo A Freedman Samuel H P Chan |
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Institution: | (1) Department of Biology, Syracuse University, 13210 Syracuse, New York |
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Abstract: | Mitochondrial cytochromec oxidase is an exceedingly complex multistructural and multifunctional membranous enzyme. In this review, we will provide an overview of the many interactions of cytochrome oxidase, stressing developments not covered by the excellent monograph of Wikström, Krab, and Saraste (1981), and continuing into early 1983. First we describe its functions (both in the nominal sense, as a transporter of electrons between cytochromec and oxygen, and in its role in energy transduction). Then we describe its structure, emphasizing the protein (its structure as a whole, the number and stoichiometry of its subunits, their biosynthetic origin, and their interactions with each other, with other components of the enzyme complex, and with the membrane as a whole). Finally, we present a model in which the protein conformation serves as the focus for the dynamic interaction of its two major functions.Abbreviations DCCD
N,N-dicyclohexylcarbodiimide
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E
m
midpoint potential
- EPR
electron paramagnetic resonance
- F1
soluble portion of the ATP synthetase complex
- NMR
nuclear magnetic resonance
- PAGE
polyacrylamide gel electrophoresis
- SDS
sodium dodecyl sulfate
- SUPAGE
SDS-urea-PAGE |
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Keywords: | Cytochrome oxidase electron transport oxidative phosphorylation lipid-protein interactions digenomic biosynthesis structural-functional interactions |
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