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Universal Features in Cytochrome Oxidase

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Cytochrome Systems

Abstract

Mitochondrial cytochrome c oxidase (cytochrome aa 3) and its equivalent in aerobic bacteria are known to be closely related in function as well as in structure (1–3). Recent cloning and sequencing of the genes for this enzyme in Paracoccus denitrificans (4,5) allows us now to make conclusions on some invariant features in cytochrome oxidase that have prevailed throughout evolution. Evolutionary conservation helps to focus the attention to the functionally most important parts in structure and guides us in attempts to make models for active centres.

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Author information

Authors and Affiliations

  1. Department of Medical Chemistry, University of Helsinki, Siltavuorenpenger 10A, SF-00170, Helsinki, Finland

    Moshe Finel, Tuomas Haltia, Liisa Holm, Tuulikki Jalli, Tuula Metso, Anne Puustinen, Mirja Raitio, Matti Saraste & Mårten Wikström

Authors
  1. Moshe Finel
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  2. Tuomas Haltia
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  3. Liisa Holm
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  4. Tuulikki Jalli
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  5. Tuula Metso
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  6. Anne Puustinen
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  7. Mirja Raitio
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  8. Matti Saraste
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  9. Mårten Wikström
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Editor information

Editors and Affiliations

  1. University of Bari, Bari, Italy

    S. Papa

  2. University of Pennsylvania, Philadelphia, Pennsylvania, USA

    B. Chance

  3. University of Stockholm, Stockholm, Sweden

    L. Ernster

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© 1987 Plenum Press, New York

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Finel, M. et al. (1987). Universal Features in Cytochrome Oxidase. In: Papa, S., Chance, B., Ernster, L. (eds) Cytochrome Systems. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1941-2_33

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  • DOI: https://doi.org/10.1007/978-1-4613-1941-2_33

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4612-9078-0

  • Online ISBN: 978-1-4613-1941-2

  • eBook Packages: Springer Book Archive

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