Structural snapshots from the oxidative half-reaction of a copper amine oxidase: Implications for O2 activation

Bryan J. Johnson; Erik T. Yukl; Valerie J. Klema; Judith P. Klinman; Carrie M. Wilmot

doi:10.1074/jbc.M113.501791

Structural snapshots from the oxidative half-reaction of a copper amine oxidase: Implications for O₂ activation

Bryan J. Johnson, Erik T. Yukl, Valerie J. Klema, Judith P. Klinman, Carrie M. Wilmot

Chemical and Structural Biology (BMBB)

Research output: Contribution to journal › Article › peer-review

18 Scopus citations

Abstract

Background: Copper amine oxidases activate O2 either at the copper center or aminoquinol cofactor. Results: Catalytic intermediates from the oxidative half-reaction are structurally and spectroscopically characterized. Conclusion: The mechanism of O2 activation may depend on accessibility dictated by two conformers of the quinone cofactor. Significance: Structural changes that inform on catalytic mechanism have been revealed in the ubiquitous copper amine oxidases.

Original language	English (US)
Pages (from-to)	28409-28417
Number of pages	9
Journal	Journal of Biological Chemistry
Volume	288
Issue number	39
DOIs	https://doi.org/10.1074/jbc.M113.501791
State	Published - Sep 27 2013

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AU - Wilmot, Carrie M.

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Structural snapshots from the oxidative half-reaction of a copper amine oxidase: Implications for O₂ activation

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