Regioselectivity in the homolytic cleavage of S-adenosylmethionine.
The observed regioselectivity of the homolytic cleavage of S-adenosylmethionine (SAM) by the radical SAM enzymes is modeled by free radical displacement reactions at sulfoxide centers. These displacements are also regioselective, in direct consequence of the reaction mechanism. The selectivity in the radical SAM reactions is explained by the geometry of the free radical displacement mechanism, required by the chemical reaction and arranged in the active site by the radical SAM proteins.
Department of Chemistry, University of Rochester, Rochester, New York 14627-0216, United States. kamp@chem.rochester.edu
Jack A
JA
Kampmeier
D005609:Free Radicals / Q000378:metabolism*; D007506:Iron-Sulfur Proteins / Q000378:metabolism*; D008780:Methyltransferases / Q000378:metabolism*; D010084:Oxidation-Reduction; D012436:S-Adenosylmethionine / Q000737:chemistry / Q000378:metabolism*; D013237:Stereoisomerism; D013454:Sulfoxides / Q000378:metabolism
D005609:Free Radicals; D007506:Iron-Sulfur Proteins; D013454:Sulfoxides; D012436:S-Adenosylmethionine; D008780:Methyltransferases