Electron Paramagnetic Resonance Spectroscopy as a Probe of Hydrogen Bonding in Heme-Thiolate Proteins
Author:
Affiliation:
1. Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, Wisconsin 53706, United States
2. Department of Chemistry, University of Michigan, 930 North University Avenue, Ann Arbor, Michigan 48109, United States
Funder
Division of Chemistry
Publisher
American Chemical Society (ACS)
Subject
Inorganic Chemistry,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.inorgchem.9b02506
Reference69 articles.
1. Functional Divergence of Heme-Thiolate Proteins: A Classification Based on Spectroscopic Attributes
2. Heme-Containing Oxygenases
3. Iron(IV)hydroxide p K a and the Role of Thiolate Ligation in C–H Bond Activation by Cytochrome P450
4. Roles of the Proximal Hydrogen Bonding Network in Cytochrome P450cam-Catalyzed Oxygenation
5. Elucidating the Role of the Proximal Cysteine Hydrogen-Bonding Network in Ferric Cytochrome P450cam and Corresponding Mutants Using Magnetic Circular Dichroism Spectroscopy
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