Binding of nitric oxide to reduced L-tryptophan-2,3-dioxygenase as studied by electron paramagnetic resonance.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference14 articles.
1. Molecular Mechanisms of Oxygen Activation;Feigelson,1974
2. Evidence for an Oxygenated Intermediate in the Tryptophan Pyrrolase Reaction
3. The Oxygenated Form of l-Tryptophan 2,3-Dioxygenase as Reaction Intermediate
4. Studies on the Interaction of Carbon Monoxide with Tryptophan Oxygenase of Pseudomonas
5. Roles of the catalytic and allosteric sites in modulating the reactivity of tryptophan oxygenase with heme ligands. I. Cyanide derivatives
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3. Nuclear Inelastic Scattering and Mössbauer Spectroscopy as Local Probes for Ligand Binding Modes and Electronic Properties in Proteins: Vibrational Behavior of a Ferriheme Center inside a β-Barrel Protein;Journal of the American Chemical Society;2012-02-27
4. EPR and Mössbauer Spectroscopy Show Inequivalent Hemes in Tryptophan Dioxygenase;Journal of the American Chemical Society;2010-01-04
5. Nitric Oxide Interaction with Insect Nitrophorins and Possibilities for the Electron Configuration of the {FeNO}6 Complex;The Smallest Biomolecules: Diatomics and their Interactions with Heme Proteins;2008
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