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Structure and evolution of cytochrome oxidase

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Abstract

The structural features of cytochrome oxidases are reviewed in light of their evolution. The substrate specificity (quinol vs. cytochromec) is reflected in the presence of a unique copper centre (Cu A ) in cytochromec oxidases. In several lines of evolution, quinol oxidases have independently lost this copper. Also, the most primitive cytochromec oxidases do not contain this copper, and electron entry takes place viac-type haems. These enzymes, exemplified by the rhizobial FixN complex, probably remind the first oxidases. They are related to the denitrification enzyme nitric oxide reductase.

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References

  1. Babcock GT & Wikström M (1992) Oxygen activation and the conservation of energy in cell respiration. Nature 356: 301–309

  2. Brown S, Moody AJ, Mitchell R & Rich PR (1993) Binuclear centre structure of terminal protonmotive oxidases. FEBS Lett. 316: 216–223

  3. Castresana J, Lübben M, Saraste M & Higgins DG (1994) Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen. EMBO J. 11: 2516–2525

  4. Garcia-Horsman JA, Berry E, Shapleigh JP, Alben JO & Gennis RB (1994) A novel cytochromec oxidase fromRhodobacter sphaeroides that lacks Cu A . Biochemistry 33: 3113–3119

  5. Gray KA, Grooms, M, Myllykallio H, Moomaw C, Slaughter C & Daldal F (1994)Rhodobacter capsulatus contains a novelcb-type cytochromec oxidase without a Cu A center. Biochemistry 33: 3120–3127

  6. Hill BC (1993) The sequence of electron carriers in the reaction of cytochromec oxidase with oxygen. J. Bioenerg. Biomembr. 25: 115–120

  7. Hosler JP, Ferguson-Miller S, Calhoun MW, Thomas JW, Hill J, Lemieux L, Ma J, Georgiou C, Fetter J, Shapleigh J, Tecklenburg MMJ, Babcock GT & Gennis RB (1993) Insight into the activesite structure and function of cytochrome oxidase by analysis of site-directed mutants of bacterial cytochromeaa 3 and cytochromebo. J. Bioenerg. Biomembr. 25: 121–136

  8. Lappalainen P, Aasa R, Malmström BG & Sarate M (1993) Soluble CuA-binding domain from theParacoccus cytochromec oxidase. J. Biol. Chem. 268: 26416–26421

  9. Malmström BG & Aasa R (1993) The nature of the Cu A center in cytochrome oxidase. FEBS Lett. 325: 49–52

  10. Preisig O, Anthamatten D & Hennecke H (1993) Genes for a microaerobically induced oxidase complex inBradyrhizobium japonicum are essential for a nitrogen-fixing endocytosis. Proc. Natl. Acad. Sci. USA 90: 3309–3313

  11. Saraste M & Castresana J (1994) Cytochrome oxidase evolved by tinkering with denitrification enzymes. FEBS Lett. 341: 1–4

  12. Saraste M, Holm L, Lemieux L, Lübben M & van der Oost J (1991) The happy family of cytochrome oxidases. Biochem. Soc. Trans. 19: 608–612

  13. Stouthamer AH (1992) Metabolic pathways inParacoccus denitrificans and closely related bacteria in relation to the phylogeny of prokaryotes. Antonic van Leeuwenhoek 61: 1–33

  14. van der Oost J, de Boer APN, de Gier J-WL, Zumft WG, Stouthamer AH & van Spanning RJM (1994) The heme-copper oxidase family consists of three distinct types of terminal oxidases and is related to nitric oxide reductase. FEMS Microbiol. Lett. (in press)

  15. Zumft WG (1993) The biological role of nitric oxide in bacteria. Arch. Microbiol. 160: 253–264

  16. Zumft WG, Dreutsch A, Löchelt S, Cuypers H, Friedrich B & Schneider B (1992) Derived amino acid sequences of thenosZ gene (respiratory N2O reductase) fromAlcaligenes eutrophus, Pseudomonas aeruginosa andPseudomonas stutzeri reveal potential copper-binding residues. Implications for the Cu A site of N2O reductase and cytochromec oxidase. Eur. J. Biochem. 208: 31–40

  17. Zumft WG, Braun C & Cuypers H (1994) Nitrix oxide reductase from Pseudomonas stutzeri, primary structure and gene organization of a novel bacterial cytochromebc complex. Eur. J. Biochem. 219: 481–490

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Saraste, M. Structure and evolution of cytochrome oxidase. Antonie van Leeuwenhoek 65, 285–287 (1994). https://doi.org/10.1007/BF00872214

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Key words

  • cytochromec oxidase
  • quinol oxidase
  • metal centres
  • respiration
  • denitrification
  • evolution