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) |
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Pages (from-to) | 28409-28417 |
Number of pages | 9 |
Journal | Journal of Biological Chemistry |
Volume | 288 |
Issue number | 39 |
DOIs | |
State | Published - Sep 27 2013 |
Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology