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A Cu(I)-semiquinone state in substrate-reduced amine oxidases

Nature volume 349, pages 262–264 (1991)Cite this article

Abstract

THE role of copper in copper-containing amine oxidases has long been a source of debate and uncertainty1. Numerous electron paramagnetic resonance (EPR) experiments2–6, including rapid freeze-quench studies7, have failed to detect changes in the copper oxidation state in the presence of substrate amines. One suggestion that copper reduction might occur8, has never been confirmed. Copper amine oxidases contain another cofactor, recently identified as 6-hydroxydopa quinone (topa quinone)9, which is reduced by substrates. Copper has been implicated in the reoxidation of the substrate-reduced enzyme10–12, but the failure to detect any copper redox change has led to proposals that Cu(II) acts as a Lewis acid13, that it has an indirect role in catalysis14, or that it serves a structural role6. We present evidence for the generation of a Cu(I)-semiquinone state by substrate reduction of several amine oxidases under anaerobic conditions, and suggest that the Cu(I)-semiquinone may be the catalytic intermediate that reacts directly with oxygen.

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Authors and Affiliations

  1. Department of Chemistry, Amherst College, Amherst, Massachusetts, 01002, USA

    David M. Dooley, Michele A. McGuirl, Doreen E. Brown & Petra N. Turowski

  2. Department of Molecular Biology, Veterans Administration Medical Center, San Francisco, California, 94121, USA

    William S. Mclntire

  3. Department of Biochemistry and Biophysics, Leeds University, Leeds, LS29JT, UK

    Peter F. Knowles

Authors
  1. David M. Dooley
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  2. Michele A. McGuirl
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  4. Petra N. Turowski
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  5. William S. Mclntire
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  6. Peter F. Knowles
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Dooley, D., McGuirl, M., Brown, D. et al. A Cu(I)-semiquinone state in substrate-reduced amine oxidases. Nature 349, 262–264 (1991). https://doi.org/10.1038/349262a0

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