Chameleon States: High-Valent Metal-Oxo Species of Cytochrome P450 and Its Ruthenium Analogue
- 2 August 2001
- journal article
- Published by Wiley in Angewandte Chemie International Edition in English
- Vol. 40 (15) , 2874-2878
- https://doi.org/10.1002/1521-3773(20010803)40:15<2874::aid-anie2874>3.0.co;2-9
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Active Iron-Oxo and Iron-Peroxo Species in Cytochromes P450 and Peroxidases; Oxo-Hydroxo Tautomerism with Water-Soluble MetalloporphyrinsPublished by Springer Nature ,2007
- The High-Valent Compound of Cytochrome P450: The Nature of the Fe−S Bond and the Role of the Thiolate Ligand as an Internal Electron DonorAngewandte Chemie, 2000
- The High-Valent Compound of Cytochrome P450: The Nature of the Fe−S Bond and the Role of the Thiolate Ligand as an Internal Electron DonorPublished by Wiley ,2000
- The Catalytic Pathway of Cytochrome P450cam at Atomic ResolutionScience, 2000
- Role of the Heme Active Site and Protein Environment in Structure, Spectra, and Function of the Cytochrome P450sChemical Reviews, 2000
- Evidence for Sulfur-Based Radicals in Thiolate Compound I IntermediatesJournal of the American Chemical Society, 1999
- Dual Role of Pyridine N-Oxides in Ruthenium Porphyrin-Catalyzed Asymmetric Epoxidation of OlefinsInorganic Chemistry, 1999
- Local Density Functional Study of Oxoiron(IV) Porphyrin Complexes and Their One-Electron Oxidized Derivatives. Axial Ligand EffectsThe Journal of Physical Chemistry A, 1997
- Delocalization over the heme and the axial ligands of one of the two oxidizing equivalents stored above the ferric state in the peroxidase and catalase Compound-I intermediates: indirect participation of the proximal axial ligand of iron in the oxidation reactions catalyzed by heme-based peroxidases and catalases?JBIC Journal of Biological Inorganic Chemistry, 1996
- Nitrous Oxide Activation by a Ruthenium PorphyrinJournal of the American Chemical Society, 1995