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Cytochrome c oxidase

C Ostermeier1, S Iwata, H Michel

  • 1Max-Planck-Institut für Biophysik, Abteilung für Molekulare Membranbiologie, Heinrich-Hoffmann-Strasse 7, 60528 Frankfurt, Germany. osti@argon.mpibp.uni-frankfurt.de

Current Opinion in Structural Biology
|August 1, 1996
PubMed
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Recent X-ray crystallography studies reveal the structures of cytochrome c oxidase from bacteria and bovine heart mitochondria. These findings provide a foundation for understanding this crucial enzyme

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biophysics

Background:

  • Cytochrome c oxidase is a vital enzyme in the respiratory chain of aerobic organisms.
  • Understanding its structure is key to elucidating its function as a proton pump.

Purpose of the Study:

  • To present the recently determined high-resolution structures of cytochrome c oxidase.
  • To provide a structural basis for understanding the enzyme's mechanism.

Main Methods:

  • X-ray crystallography was used to determine the structures.
  • Resolution achieved was 2.8 Å for both bacterial and bovine enzymes.

Main Results:

  • The detailed structures of cytochrome c oxidase from *Paracoccus denitrificans* were reported.

Related Experiment Videos

  • The structures of the metal centers within bovine heart mitochondrial cytochrome c oxidase were elucidated.

    • Conclusions:

    • The reported structures offer critical insights into the mechanism of this redox-coupled proton pump.
    • These structural data are fundamental for comprehending cellular respiration in aerobic life.