Spectroscopic and Electronic Structure Description of the Reduced Binuclear Non-Heme Iron Active Site in Ribonucleotide Reductase from E. coli: Comparison to Reduced Δ9 Desaturase and Electronic Structure Contributions to Differences in O2 Reactivity
Author:
Affiliation:
1. Contribution from the Department of Chemistry, Stanford University, Stanford, California 94305, and the 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/ja994406r
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1. Dioxygen and Hemerythrin
2. Dioxygen Activation by Enzymes Containing Binuclear Non-Heme Iron Clusters
3. Recombinant Toluene-4-monooxygenase: Catalytic and Mössbauer Studies of the Purified Diiron and Rieske Components of a Four-Protein Complex
4. DESATURATION AND RELATED MODIFICATIONS OF FATTY ACIDS
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