Interdomain Long-Range Electron Transfer Becomes Rate-Limiting in the Y216A Variant of Tyramine β-Monooxygenase
Author:
Affiliation:
1. Department of Science and Engineering, School of Medicine, Oregon Health and Sciences University, Beaverton, Oregon 97006, United States
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi3013609
Reference42 articles.
1. The Copper-Enzyme Family of Dopamine β-Monooxygenase and Peptidylglycine α-Hydroxylating Monooxygenase: Resolving the Chemical Pathway for Substrate Hydroxylation
2. The Catalytic Core of Peptidylglycine .alpha.-Hydroxylating Monooxygenase: Investigation by Site-Directed Mutagenesis, Cu X-ray Absorption Spectroscopy, and Electron Paramagnetic Resonance
3. Expression and characterization of recombinant tyramine β-monooxygenase from Drosophila: A monomeric copper-containing hydroxylase
4. Amidation of Bioactive Peptides: The Structure of Peptidylglycine α-Hydroxylating Monooxygenase
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