Radical SAM Enzyme Spore Photoproduct Lyase: Properties of the Ω Organometallic Intermediate and Identification of Stable Protein Radicals Formed during Substrate-Free Turnover
Author:
Affiliation:
1. Department of Chemistry & Biochemistry, Montana State University, Bozeman, Montana. 59717, United States
2. Department of Chemistry, Northwestern University, Evanston, Illinois 60208, United States
Funder
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/jacs.0c08585
Reference52 articles.
1. Radical S-Adenosylmethionine Enzymes
2. The Radical SAM Superfamily
3. Atlas of the Radical SAM Superfamily: Divergent Evolution of Function Using a “Plug and Play” Domain
4. An Anchoring Role for FeS Clusters: Chelation of the Amino Acid Moiety of S-Adenosylmethionine to the Unique Iron Site of the [4Fe−4S] Cluster of Pyruvate Formate-Lyase Activating Enzyme
5. Electron-Nuclear Double Resonance Spectroscopic Evidence That S-Adenosylmethionine Binds in Contact with the Catalytically Active [4Fe−4S]+ Cluster of Pyruvate Formate-Lyase Activating Enzyme
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1. ENDOR Spectroscopy Reveals the “Free” 5′-Deoxyadenosyl Radical in a Radical SAM Enzyme Active Site Actually is Chaperoned by Close Interaction with the Methionine-Bound [4Fe–4S]2+ Cluster;Journal of the American Chemical Society;2024-02-03
2. Pyruvate formate-lyase activating enzyme: The catalytically active 5′-deoxyadenosyl radical caught in the act of H-atom abstraction;Proceedings of the National Academy of Sciences;2023-11-13
3. Mechanism of Radical Initiation in the Radical SAM Enzyme Superfamily;Annual Review of Biochemistry;2023-06-20
4. Mechanism of Radical S-Adenosyl-l-methionine Adenosylation: Radical Intermediates and the Catalytic Competence of the 5′-Deoxyadenosyl Radical;Journal of the American Chemical Society;2022-03-08
5. Broken-Symmetry Density Functional Theory Analysis of the Ω Intermediate in Radical S-Adenosyl-l-methionine Enzymes: Evidence for a Near-Attack Conformer over an Organometallic Species;Journal of the American Chemical Society;2022-02-16
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