Dph3 Enables Aerobic Diphthamide Biosynthesis by Donating One Iron Atom to Transform a [3Fe–4S] to a [4Fe–4S] Cluster in Dph1–Dph2
Author:
Affiliation:
1. Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, United States
2. Howard Hughes Medical Institute, Cornell University, Ithaca, New York 14853, 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.1c03956
Reference29 articles.
1. Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods
2. Radical S-Adenosylmethionine Enzymes
3. Iron-sulphur clusters and the problem with oxygen
4. Diphthamide biosynthesis requires an organic radical generated by an iron–sulphur enzyme
5. Dph3 Is an Electron Donor for Dph1-Dph2 in the First Step of Eukaryotic Diphthamide Biosynthesis
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