Abstract

The reaction mechanisms of oxidative degradation of the anaerobic radical enzyme pyruvate formate-lyase (PFL) have been examined at the theoretical hybrid Hartree−Fock/density functional theory level B3-LYP. It is concluded that the most likely scenario involves O2 addition at the glycyl radical site, followed by H• abstraction/transfer from C419 and subsequent rearrangements to generate an α-hydroxyglycine and the sulfinyl radical R−SO•, observed by EPR spectroscopy. In addition, the present model accounts for alternative fragmentations observed in wild-type PFL, and the formation and degradation of Gly−O-O• in the absence of C419 (as observed in C419A and C419AC418A mutants).

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