Model for the Cofactor Formation Reaction of E. Coli Ribonucleotide Reductase. From a Diiron(II) Precursor to an FeIIIFeIV Species via a Peroxo Intermediate-Reference-Cited by-同舟云学术

Model for the Cofactor Formation Reaction of E. Coli Ribonucleotide Reductase. From a Diiron(II) Precursor to an FeIIIFeIV Species via a Peroxo Intermediate

Published:2000-05-01 Issue:11 Volume:39 Page:2254-2255
ISSN:0020-1669
Container-title:Inorganic Chemistry
language:en
Short-container-title:Inorg. Chem.

Author:

MacMurdo Vicki L.¹,Zheng Hui¹,Que Lawrence¹

Affiliation:

1. Department of Chemistry and Center for Metals in Biocatalysis, University of Minnesota, Minneapolis, Minnesota 55455

Publisher

American Chemical Society (ACS)

Subject

Inorganic Chemistry,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/ic991482m

Reference30 articles.

1. Harnessing free radicals: formation and function of the tyrosyl radical in ribonucleotide reductase

2. Dioxygen Activation by Enzymes Containing Binuclear Non-Heme Iron Clusters

3. Mechanism of Assembly of the Tyrosyl Radical-Dinuclear Iron Cluster Cofactor of Ribonucleotide Reductase

4. Engineering the Diiron Site of Escherichia coli Ribonucleotide Reductase Protein R2 to Accumulate an Intermediate Similar to Hperoxo, the Putative Peroxodiiron(III) Complex from the Methane Monooxygenase Catalytic Cycle

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