Formally Copper(III)–Alkylperoxo Complexes as Models of Possible Intermediates in Monooxygenase Enzymes
Author:
Affiliation:
1. Department of Chemistry and Center for Metals in Biocatalysis, University of Minnesota, 207 Pleasant Street SE, Minneapolis, Minnesota 55455, United States
Funder
Division of Chemistry
National Institutes of Health
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/jacs.7b05754
Reference42 articles.
1. Copper Active Sites in Biology
2. Aerobic Copper-Catalyzed Organic Reactions
3. Copper-Catalyzed Aerobic Oxidative CH Functionalizations: Trends and Mechanistic Insights
4. The Copper-Enzyme Family of Dopamine β-Monooxygenase and Peptidylglycine α-Hydroxylating Monooxygenase: Resolving the Chemical Pathway for Substrate Hydroxylation
5. Oxygen Activation by the Noncoupled Binuclear Copper Site in Peptidylglycine α-Hydroxylating Monooxygenase. Reaction Mechanism and Role of the Noncoupled Nature of the Active Site
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