Deconvoluting the Reduction Potentials for the Three [4Fe-4S] Clusters in an AdoMet Radical SCIFF Maturase
Author:
Affiliation:
1. Department of Chemistry, Boston University, 590 Commonwealth Avenue, Boston, Massachusetts 02215, United States
2. Department of Chemistry, University of Utah, 315 South 1400 East, Salt Lake City, Utah 84112, United States
Funder
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
http://pubs.acs.org/doi/pdf/10.1021/acs.biochem.8b00846
Reference22 articles.
1. Using the Structure‐Function Linkage Database to Characterize Functional Domains in Enzymes
2. 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
3. Coordination and Mechanism of Reversible Cleavage of S-Adenosylmethionine by the [4Fe-4S] Center in Lysine 2,3-Aminomutase
4. Identification and function of auxiliary iron–sulfur clusters in radical SAM enzymes
5. Auxiliary iron–sulfur cofactors in radical SAM enzymes
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