Abstract

Abstract: Pyruvate formate-lyase, a homodimeric protein of 2 × 85 kDa, is distinguished by the property of containing a stable organic free radical (g = 2.0037) in its structure. The enzyme catalyzes pyruvate conversion to acetyl-CoA via two distinct half-reactions (E-SH + pyruvate ⇌ E-S-acetyl + formate; E-S-acetyl + CoA ⇌ E-SH + acetyl-CoA), the first of which has been proposed to occur through reversible carbon-carbon bond cleavage by a homolytic mechanism (1).

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