Cluster-selective 57Fe labeling of a Twitch-domain-containing radical SAM enzyme
Author:
Affiliation:
1. Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA
Abstract
Funder
National Institutes of Health
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2023/SC/D3SC02016A
Reference43 articles.
1. Radical S-Adenosylmethionine Enzymes
2. Atlas of the Radical SAM Superfamily: Divergent Evolution of Function Using a “Plug and Play” Domain
3. RadicalSAM.org: A Resource to Interpret Sequence-Function Space and Discover New Radical SAM Enzyme Chemistry
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. Coordination of Adenosylmethionine to a Unique Iron Site of the [4Fe-4S] of Pyruvate Formate-Lyase Activating Enzyme: A Mössbauer Spectroscopic Study
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1. Metal–Metal Redox Exchange to Produce Heterometallic Manganese–Cobalt Oxo Cubanes via a “Dangler” Intermediate;Journal of the American Chemical Society;2024-07-09
2. Twitch Radical S ‐adenosyl‐ l ‐methionine Alcohol Dehydrogenases;Encyclopedia of Inorganic and Bioinorganic Chemistry;2024-04
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