Dioxygenases without requirement for cofactors and their chemical model reaction: compulsory order ternary complex mechanism of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase involving general base catalysis by histidine 251 and single-electron oxidation of the substrate dianion. [electronic resource]
Producer: 20050111Description: 14485-99 p. digitalISSN:- 0006-2960
- Alanine -- genetics
- Anaerobiosis -- genetics
- Arthrobacter -- enzymology
- Bacterial Proteins -- antagonists & inhibitors
- Binding Sites
- Catalysis
- Dioxygenases -- antagonists & inhibitors
- Electron Spin Resonance Spectroscopy
- Electrons
- Enzyme Activation -- genetics
- Escherichia coli Proteins -- chemistry
- Histidine -- chemistry
- Hydrogen Peroxide -- chemistry
- Hydrogen-Ion Concentration
- Kinetics
- Models, Chemical
- Mutagenesis, Site-Directed
- Oxidation-Reduction
- Oxygen -- chemistry
- Quinaldines -- chemistry
- Spectrophotometry, Ultraviolet
- Substrate Specificity
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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