Radicals in enzymatic reactions.
Spectroscopic and kinetic evidence for substrate-based radicals in the reactions of lysine 2,3-aminomutase and methane monooxygenase has recently been gathered. Evidence for a protein-based thiyl radical in the mechanism of the action of ribonucleotide reductase has been correlated with the proposed mechanism involving substrate-based radicals. Controversies have arisen about the mechanisms of ribonucleotide reductase and methane monooxygenase reactions.
Institute for Enzyme Research, University of Wisconsin-Madison, 1710 University Avenue, Madison, WI 53705, USA. frey@enzyme.wisc.edu
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D003038:Cobamides / Q000378:metabolism; D005609:Free Radicals; D019751:Intramolecular Transferases / Q000378:metabolism*; D010105:Oxygenases / Q000378:metabolism*; D012264:Ribonucleotide Reductases / Q000378:metabolism*; D013379:Substrate Specificity; D013438:Sulfhydryl Compounds / Q000378:metabolism*
D003038:Cobamides; D005609:Free Radicals; D013438:Sulfhydryl Compounds; D010105:Oxygenases; C021555:methane monooxygenase; D012264:Ribonucleotide Reductases; D019751:Intramolecular Transferases; C021518:lysine 2,3-aminomutase; C000913:cobamamide