X‐ray Crystal Structures of Cytochrome c Oxidases from Paracoccus denitrificans and Bovine Heart and Their Implications for the Molecular Mechanism of Cell Respiration
Bernhard Kadenbach
Abstract
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Bernhard Kadenbach
Abstract
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Pores with rotational symmetry, each formed from five transmembrane helices in cytochrome c oxidase, form the postulated pathways for the protons required for the biochemical reduction of O2 as well as for the protons transported across the cell (or inner mitochondrial) membrane resulting in a H+ gradient. The structures of cytochrome c oxidase from a bacterium recently described by Michel et al. and from bovine heart by Yoshikawa et al. corroborate many previous results on the structure and function of this enzyme and disprove others.
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Pores with rotational symmetry, each formed from five transmembrane helices in cytochrome c oxidase, form the postulated pathways for the protons required for the biochemical reduction of O2 as well as for the protons transported across the cell (or inner mitochondrial) membrane resulting in a H+ gradient. The structures of cytochrome c oxidase from a bacterium recently described by Michel et al. and from bovine heart by Yoshikawa et al. corroborate many previous results on the structure and function of this enzyme and disprove others.
Key concepts: Paracoccus denitrificans, Cytochrome c oxidase, Electron Transport Complex IV, Cytochrome c, Cytochrome, Oxidase test, Enzyme, Respiratory chain