Spectroscopic and equilibrium studies of ligand and organic substrate binding to indolamine 2,3-dioxygenase
- 13 February 1990
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 29 (6), 1451-1460
- https://doi.org/10.1021/bi00458a016
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 26 references indexed in Scilit:
- Formation of low spin complexes of ferric cytochrome P-450-CAM with anionic ligands. Spin state and ligand affinity comparison to myoglobin.Journal of Biological Chemistry, 1982
- Copper is not essential for the catalytic activity of L-tryptophan 2,3-dioxygenase.Journal of Biological Chemistry, 1980
- Indoleamine 2,3-dioxygenase. Equilibrium studies of the tryptophan binding to the ferric, ferrous, and CO-bound enzymes.Journal of Biological Chemistry, 1980
- Indoleamine 2,3-dioxygenase. Kinetic studies on the binding of superoxide anion and molecular oxygen to enzyme.Journal of Biological Chemistry, 1979
- Electron transfer from pyridinyl radicals, hydrated electrons, CO2•- and O2•- bacterial cytochrome P450Biochemical and Biophysical Research Communications, 1979
- Indoleamine 2,3-dioxygenase. Purification and some propertiesJournal of Biological Chemistry, 1978
- Indoleamine 2,3-dioxygenase. Characterization and properties of enzyme. O2- complex.Journal of Biological Chemistry, 1977
- One electron reduction of metmyoglobin and methemoglobin and the reaction of the reduced molecule with oxygenBiochimica et Biophysica Acta (BBA) - Protein Structure, 1976
- The kinetics of formation of horseradish peroxidase compound I by reaction with peroxobenzoic acids. pH and peroxo acid substituent effectsBiochemical Journal, 1976
- The Kinetics of Fluoride Binding by Ferric Horse Radish Peroxidase*Biochemistry, 1967