Capturing the Binuclear Copper State of Peptidylglycine Monooxygenase Using a Peptidyl-Homocysteine Lure
Author:
Affiliation:
1. Department of Chemical Physiology and Biochemistry, Oregon Health & Science University, Portland, Oregon 97239, United States
2. Department of Chemistry, University of Utah, Salt Lake City, Utah 84112, United States
Funder
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Link
https://pubs.acs.org/doi/pdf/10.1021/jacs.3c14705
Reference68 articles.
1. The Copper-Enzyme Family of Dopamine β-Monooxygenase and Peptidylglycine α-Hydroxylating Monooxygenase: Resolving the Chemical Pathway for Substrate Hydroxylation
2. Copper monooxygenase reactivity: Do consensus mechanisms accurately reflect experimental observations?
3. Biochemistry of aerobic biological methane oxidation
4. Lytic polysaccharide monooxygenases and other histidine-brace copper proteins: structure, oxygen activation and biotechnological applications
5. Capture of activated dioxygen intermediates at the copper-active site of a lytic polysaccharide monooxygenase
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