Nature of the Peroxo Intermediate of the W48F/D84E Ribonucleotide Reductase Variant: Implications for O2 Activation by Binuclear Non-Heme Iron Enzymes-Reference-Cited by-同舟云学术

Nature of the Peroxo Intermediate of the W48F/D84E Ribonucleotide Reductase Variant: Implications for O2 Activation by Binuclear Non-Heme Iron Enzymes

Published:2004-06-22 Issue:28 Volume:126 Page:8842-8855
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Skulan Andrew J.¹,Brunold Thomas C.¹,Baldwin Jeffrey¹,Saleh Lana¹,Bollinger, J. Martin¹,Solomon Edward I.¹

Affiliation:

1. Contribution from the Department of Chemistry, Stanford University, Stanford, California 94305, and Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja049106a

Reference71 articles.

1. Ribonucleotide Reductase—a Radical Enzyme

2. Geometric and Electronic Structure/Function Correlations in Non-Heme Iron Enzymes

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

4. Involvement of Ferredoxin in Desaturation of Lipid-Bound Oleate in Chloroplasts

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