Evidence Against Reduction of Cu2+ to Cu+ during Dioxygen Activation in a Copper Amine Oxidase from Yeast
Author:
Affiliation:
1. Contribution from the Department of Chemistry and the Department of Molecular and Cell Biology, University of California, Berkeley, California 94720
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja000325f
Reference34 articles.
1. An investigation of bovine serum amine oxidase active site stoichiometry: evidence for an aminotransferase mechanism involving two carbonyl cofactors per enzyme dimer
2. Mutation of a Strictly Conserved, Active-Site Residue Alters Substrate Specificity and Cofactor Biogenesis in a Copper Amine Oxidase
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