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Multicopper oxidases: intramolecular electron transfer and O2 reduction

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Abstract

The multicopper oxidases are an intriguing, widespread family of enzymes that catalyze the reduction of O2 to water by a variety of single-electron and multiple-electron reducing agents. The structure and properties of the copper binding sites responsible for the latter chemical transformations have been studied for over 40 years and a detailed picture is emerging. This review focuses particularly on the kinetics of internal electron transfer between the type 1 (blue) copper site and the trinuclear center, as well as on the nature of the intermediates formed in the oxygen reduction process.

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Acknowledgment

O.F. thanks the Kimmelman Center for Biomolecular Structure and Assembly at the Weizmann Institute of Science for generous support.

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Authors and Affiliations

  1. Department of Chemistry, Washington State University, Pullman, WA, 99164-4630, USA

    Scot Wherland

  2. Department of Analytic and Bioinorganic Chemistry, University of Copenhagen, 2100, Copenhagen Ø, Denmark

    Ole Farver

  3. Department of Immunology, The Weizmann Institute of Science, 76100, Rehovot, Israel

    Israel Pecht

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  1. Scot Wherland
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  2. Ole Farver
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  3. Israel Pecht
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Correspondence to Israel Pecht.

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Responsible Editors: Lucia Banci and Claudio Luchinat.

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Wherland, S., Farver, O. & Pecht, I. Multicopper oxidases: intramolecular electron transfer and O2 reduction. J Biol Inorg Chem 19, 541–554 (2014). https://doi.org/10.1007/s00775-013-1080-7

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