Conformationally Dynamic Radical Transfer within Ribonucleotide Reductase.

doi:10.1021/jacs.7b08192

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Article

Conformationally Dynamic Radical Transfer within Ribonucleotide Reductase.

Journal of the American Chemical Society - 22 Nov 2017

Greene Brandon L, Taguchi Alexander T, Stubbe JoAnne, Nocera Daniel G

Abstract excerpt

Ribonucleotide reductases (RNR) catalyze the reduction of nucleotides to deoxynucleotides through a mechanism involving an essential cysteine based thiyl radical. In the E. coli class 1a RNR the thiyl radical (C439•) is a transient species generated by radical transfer (RT) from a stable diferric-tyrosyl radical cofactor located >35 Å away across the α2:β2 subunit interface. RT is facilitated by sequential...

Topics

Electrons
Escherichia coli
Free Radicals
Hydrogen Bonding
Kinetics
Models, Molecular
Mutation
Oxidation-Reduction
Protons
Reproducibility of Results
Ribonucleotide Reductases
Tyrosine

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Identifiers

PMID: 29037038
DOI: 10.1021/jacs.7b08192
PMCID: PMC5702266

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