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Effect of pH and Temperature on Electron Transfer in Mixed-Valence Cytochrome c Oxidase

  • Peter Brzezinski
  • Bo G. Malmström

Abstract

Cytochrome c oxidase is the terminal, dioxygen-reducing enzyme in the respiratory chain of mitochondria. The enzyme contains four active metal centers. Two heme groups (cytochrome a and a3) and two copper ions (CuA and CuB). Cytochrome oxidase catalyzes a vectorial reaction in which electron transport is coupled to the translocation of protons from the matrix to the cytosol side of the inner mitochondrial membrane (1–3). The requirement of such a pump is that it can exist in two different conformations with different access for protons to the two sides of the membrane. The pump must also control the electron flow through the protein. Such electron gating requires that reduction and the subsequent oxidation of certain metal centers in the protein must take place in different conformations (1, 2).

Keywords

Metal Center Cytochrome Oxidase Electron Flow Slow Phase Heme Group 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Peter Brzezinski
    • 1
    • 2
  • Bo G. Malmström
    • 1
    • 2
  1. 1.Department of Biochemistry and BiophysicsChalmers University of TechnologyGöteborgSweden
  2. 2.University of GöteborgGöteborgSweden

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