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Insight into the active-site structure and function of cytochrome oxidase by analysis of site-directed mutants of bacterial cytochromeaa 3 and cytochromebo

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Abstract

Cytochromeaa 3 ofRhodobacter sphaeroides and cytochromebo ofE. coli are useful models of the more complex cytochromec oxidase of eukaryotes, as demonstrated by the genetic, spectroscopic, and functional studies reviewed here. A summary of site-directed mutants of conserved residues in these two enzymes is presented and discussed in terms of a current model of the structure of the metal centers and evidence for regions of the protein likely to be involved in proton transfer. The model of ligation of the hemea 3 (oro)-CuB center, in which both hemes are bound to helix X of subunit I, has important implications for the pathways and control of electron transfer.

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Author notes

  1. James Shapleigh

    Present address: Section of Microbiology, Cornell University, Wing Hall, 14853, Ithaca, New York

  2. Mary M. J. Tecklenburg

    Present address: Department of Chemistry, Central Michigan University, 48859, Mt. Pleasant, Michigan

Authors and Affiliations

  1. Departments of Biochemistry and Chemistry, Michigan State University, 48824, East Lansing, Michigan

    Jonathan P. Hosler, Shelagh Ferguson-Miller, John Fetter, Mary M. J. Tecklenburg & Gerald T. Babcock

  2. School of Chemical Sciences, University of Illinois, 61801, Urbana, Illinois

    Melissa W. Calhoun, Jeffrey W. Thomas, John Hill, Laura Lemieux, Jixiang Ma, Christos Georgiou, James Shapleigh & Robert B. Gennis

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  1. Jonathan P. Hosler
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  2. Shelagh Ferguson-Miller
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Hosler, J.P., Ferguson-Miller, S., Calhoun, M.W. et al. Insight into the active-site structure and function of cytochrome oxidase by analysis of site-directed mutants of bacterial cytochromeaa 3 and cytochromebo . J Bioenerg Biomembr 25, 121–136 (1993). https://doi.org/10.1007/BF00762854

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