Studies on the roles of the catalytic and allosteric sites in modulating the reactivity of tryptophan oxygenase with heme ligands. I. Cyanide derivatives.
D000494:Allosteric Regulation; D001665:Binding Sites; D002384:Catalysis; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003486:Cyanides; D004578:Electron Spin Resonance Spectroscopy; D005461:Fluorine; D006146:Guanidines; D006418:Heme; D006851:Hydrochloric Acid; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D046911:Macromolecular Substances; D009570:Nitriles; D010084:Oxidation-Reduction; D010544:Peroxidases; D010944:Plants / Q000201:enzymology; D011188:Potassium; D011485:Protein Binding; D011487:Protein Conformation; D011489:Protein Denaturation; D011549:Pseudomonas / Q000201:enzymology*; D013053:Spectrophotometry; D013447:Sulfites; D014364:Tryptophan; D014366:Tryptophan Oxygenase / Q000037:antagonists & inhibitors
D003486:Cyanides; D006146:Guanidines; D046911:Macromolecular Substances; D009570:Nitriles; D013447:Sulfites; D005461:Fluorine; D006418:Heme; D014364:Tryptophan; D010544:Peroxidases; D014366:Tryptophan Oxygenase; D006851:Hydrochloric Acid; D011188:Potassium