The Heme–Lys Cross-Link in Cytochrome P460 Promotes Catalysis by Enforcing Secondary Coordination Sphere Architecture
Author:
Affiliation:
1. Baker Laboratory, Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, United States
Funder
Office of Science
National Institutes of Health
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.0c00261
Reference50 articles.
1. Mössbauer, EPR, and optical studies of the P-460 center of hydroxylamine oxidoreductase from Nitrosomonas. A ferrous heme with an unusually large quadrupole splitting.
2. The Crystal Structure of Cytochrome P460 ofNitrosomonas europaeaReveals a Novel Cytochrome Fold and Heme−Protein Cross-link,
3. CytochromecBiogenesis: Mechanisms for Covalent Modifications and Trafficking of Heme and for Heme-Iron Redox Control
4. The Eponymous Cofactors in Cytochrome P460s from Ammonia-Oxidizing Bacteria Are Iron Porphyrinoids Whose Macrocycles Are Dibasic
5. Structural Studies of Hydroxylamine Oxidoreductase Reveal a Unique Heme Cofactor and a Previously Unidentified Interaction Partner
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1. Cytochrome P460 Cofactor Maturation Proceeds via Peroxide-Dependent Post-translational Modification;Journal of the American Chemical Society;2023-06-20
2. Outer coordination sphere influences on cofactor maturation and substrate oxidation by cytochrome P460;Chemical Science;2023
3. The Biologically Relevant Coordination Chemistry of Iron and Nitric Oxide: Electronic Structure and Reactivity;Chemical Reviews;2021-12-13
4. A novel catalytic heme cofactor in SfmD with a single thioether bond and a bis-His ligand set revealed by a de novo crystal structural and spectroscopic study;Chemical Science;2021
5. Heme P460: A (Cross) Link to Nitric Oxide;Accounts of Chemical Research;2020-11-12
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