Spectroscopic Definition of the Ferroxidase Site in M Ferritin: Comparison of Binuclear Substrate vs Cofactor Active Sites
Author:
Affiliation:
1. Department of Chemistry, Stanford University, 333 Campus Drive, Stanford, California 94305, and Center for BioIron at CHORI (Children’s Hospital Oakland Research Institute), 747 52nd Street, Oakland, California 94609
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja801251q
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1. Circular Dichroism and Magnetic Circular Dichroism Studies of the Reduced Binuclear Non-Heme Iron Site of Stearoyl-ACP Δ9-Desaturase: Substrate Binding and Comparison to Ribonucleotide Reductase
2. Spectroscopic studies of the coupled binuclear non-heme iron active site in the fully reduced hydroxylase component of methane monooxygenase: comparison to deoxy and deoxy-azide hemerythrin
3. Electronic and Spectroscopic Studies of the Non-Heme Reduced Binuclear Iron Sites of Two Ribonucleotide Reductase Variants: Comparison to Reduced Methane Monooxygenase and Contributions to O2 Reactivity
4. 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
5. Crystal Structures of the Soluble Methane Monooxygenase Hydroxylase from Methylococcus capsulatus (Bath) Demonstrating Geometrical Variability at the Dinuclear Iron Active Site
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