Accumulation and Pulse Electron Paramagnetic Resonance Spectroscopic Investigation of the 4-Oxidobenzyl Radical Generated in the Radical S-Adenosyl-l-methionine Enzyme HydG
Author:
Affiliation:
1. Department of Chemistry, University of California Davis, Davis, California 95616, United States
Funder
Army Research Office
National Institutes of Health
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.1c00619
Reference67 articles.
1. Radical S-Adenosylmethionine Enzymes
2. Structure–function relationships of radical SAM enzymes
3. Radical SAM catalysis via an organometallic intermediate with an Fe–[5′-C]-deoxyadenosyl bond
4. Paradigm Shift for Radical S-Adenosyl-l-methionine Reactions: The Organometallic Intermediate Ω Is Central to Catalysis
5. The Elusive 5′-Deoxyadenosyl Radical: Captured and Characterized by Electron Paramagnetic Resonance and Electron Nuclear Double Resonance Spectroscopies
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1. A Conserved Binding Pocket in HydF is Essential for Biological Assembly and Coordination of the Diiron Site of [FeFe]-Hydrogenases;Journal of the American Chemical Society;2024-05-31
2. Radical SAM Enzyme PylB Generates a Lysyl Radical Intermediate in the Biosynthesis of Pyrrolysine by Using SAM as a Cofactor;Journal of the American Chemical Society;2024-03-01
3. Characterizing the Biosynthesis of the [Fe(II)(CN)(CO)2(cysteinate)]− Organometallic Product of the Radical-SAM Enzyme HydG by EPR and Mössbauer Spectroscopy;The Journal of Physical Chemistry B;2023-10-20
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5. The [4Fe‐4S]‐Cluster of HydF is not Required for the Binding and Transfer of the Diiron Site of [FeFe]‐Hydrogenases;ChemBioChem;2023-05-04
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