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Reaction of AdoMet with ThiC generates a backbone free radical.

ABSTRACT: ThiC is an [4Fe-4S] cluster protein that catalyzes the formation of 4-amino-5-hydroxymethyl-2-methylpyrimidine. EPR spectroscopic studies demonstrate that, upon interaction with AdoMet, active ThiC from Salmonella enterica generates a persistent free radical on the alpha-carbon of an amino acid residue. The EPR properties of the radical are consistent with any residue other than a Gly or Ala. Exposure to oxygen was accompanied by a fission of the radical-carrying polypeptide chain between the Gly436 and His437 residues in ThiC. Regardless of whether the backbone radical is part of the catalytic machinery, its presence provides evidence that ThiC employs free radical chemistry as expected for radical SAM enzymes.

SUBMITTER: Martinez-Gomez NC

PROVIDER: S-EPMC2654281 | biostudies-literature | 2009 Jan

REPOSITORIES: biostudies-literature

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Reaction of AdoMet with ThiC generates a backbone free radical.

Martinez-Gomez N Cecilia NC Poyner Russell R RR Mansoorabadi Steven O SO Reed George H GH Downs Diana M DM

Biochemistry 20090101 2

ThiC is an [4Fe-4S] cluster protein that catalyzes the formation of 4-amino-5-hydroxymethyl-2-methylpyrimidine. EPR spectroscopic studies demonstrate that, upon interaction with AdoMet, active ThiC from Salmonella enterica generates a persistent free radical on the alpha-carbon of an amino acid residue. The EPR properties of the radical are consistent with any residue other than a Gly or Ala. Exposure to oxygen was accompanied by a fission of the radical-carrying polypeptide chain between the Gl ...[more]

PMID: 19113839

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