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Relationship of Cytochrome caa3 from Thermus thermophilus to Other Heme- and Copper-Containing Terminal Oxidases

  • M. W. Mather
  • P. Springer
  • J. A. Fee
Part of the 41. Colloquium der Gesellschaft für Biologische Chemie 5.–7. April 1990 in Mosbach/Baden book series (MOSBACH, volume 41)

Abstract

Cytochrome oxidases are a key component of the energy metabolism of most aerobic organisms from mammals to bacteria. They are the final enzyme of the membrane-associated respiratory chain responsible for converting the chemical energy of reduced substrates to a transmembrane electrochemical potential, which is used by the cell for a wide variety of energy-requiring processes. The most widely studied oxidase is the cytochrome c oxidase (cytochrome aa3 oxidase) of the mammalian mitochondrion. This complex, integral membrane protein contains 13 subunits and 4 canonical metal centers : heme centers, a and a3 ; copper centers, CuA and CuB. It is responsible for electron transfer from reduced cytochrome c to dioxygen with the concomitant reduction of dioxygen to water and the coupled vectorial transfer of protons across the mitochondrial membrane (see Chan and Li 1990; Palmer 1987 for recent reviews).

Keywords

Oxidase Subunit Hydrophobic Segment Paracoccus Denitrificans Thermus Thermophilus Quinol Oxidase 
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

© Springer-Verlag Berlin Heidelberg 1990

Authors and Affiliations

  • M. W. Mather
  • P. Springer
  • J. A. Fee
    • 1
  1. 1.Biochemistry Section and Stable Isotope ResourceIsotope and Structural Chemistry Group, Los Alamos National LaboratoryLos AlamosUSA

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