Radical-Translocation Intermediates and Hurdling of Pathway Defects in “Super-oxidized” (MnIV/FeIV) Chlamydia trachomatis Ribonucleotide Reductase
Author:
Affiliation:
1. Departments of Biochemistry and Molecular Biology and ‡Chemistry, The Pennsylvania State University, University Park, Pennsylvania 16802, United States
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja309468s
Reference73 articles.
1. Ribonucleotide Reductases
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3. On the mechanism of ribonucleoside diphosphate reductase from Escherichia coli. Evidence for 3'-C–H bond cleavage.
4. Characterization of C439SR1, a mutant of Escherichia coli ribonucleotide diphosphate reductase: evidence that C439 is a residue essential for nucleotide reduction and C439SR1 is a protein possessing novel thioredoxin-like activity
5. Radical Initiation in the Class I Ribonucleotide Reductase: Long-Range Proton-Coupled Electron Transfer?
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