Adenosylmethionine as a source of 5'-deoxyadenosyl radicals.
The combination of an iron-sulfur cluster and S-adenosylmethionine provides a novel mechanism for the initiation of radical catalysis in an unanticipated variety of metabolic processes. Molecular details of the cluster-mediated reductive cleavage of S-adenosylmethionine to methionine and, presumably, a 5'-deoxyadenosyl radical are the targets of recent studies.
Fontecave
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Laboratoire de Chimie et Biochimie des Centres Rédox Biologiques, DBMS-CB, CEA/CNRS/Université Joseph Fourier, UMR 5047, 17 Avenue des Martyrs, 38054 Grenoble, Cedex 09, France. mfontecave@cea.fr
Mulliez
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Ollagnier-de-Choudens
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D000693:Anaerobiosis; D001426:Bacterial Proteins; D001665:Binding Sites; D003839:Deoxyadenosines / Q000737:chemistry*; D005609:Free Radicals; D019751:Intramolecular Transferases / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000737:chemistry / Q000378:metabolism; D008956:Models, Chemical; D012436:S-Adenosylmethionine / Q000737:chemistry* / Q000378:metabolism
D001426:Bacterial Proteins; D003839:Deoxyadenosines; D005609:Free Radicals; D007506:Iron-Sulfur Proteins; C408542:nrdG protein, Lactococcus lactis; D012436:S-Adenosylmethionine; D019751:Intramolecular Transferases; C021518:lysine 2,3-aminomutase