Radical SAM enzymes: surprises along the path to understanding mechanism

J Biol Inorg Chem. 2019 Sep;24(6):769-776. doi: 10.1007/s00775-019-01706-w. Epub 2019 Sep 7.

Abstract

As the field of radical SAM enzymology has grown from a few examples in the 1990s to hundreds of thousands today, a fundamental question has remained: how does Nature use S-adenosyl-L-methionine to initiate radical reactions? This was a driving question when we first began studying pyruvate formate-lyase activating enzyme in 1993, and our journey for answers has brought us to many surprising discoveries, from the direct coordination of SAM to a unique iron in a [4Fe-4S] cluster, to our recent discovery of an organometallic intermediate and our ability to quantitatively produce and characterize the long-sought 5'-deoxyadenosyl radical intermediate. These adventures and what we have learned along the way about this fundamentally novel chemistry is described in this review.

Keywords: Deoxyadenosyl radical; Organometallic; Radical SAM; S-adenosylmethionine.

Publication types

  • Review

MeSH terms

  • Acetyltransferases / metabolism
  • Iron-Sulfur Proteins / chemistry*
  • Iron-Sulfur Proteins / metabolism
  • Molecular Structure
  • Oxidation-Reduction
  • S-Adenosylmethionine / chemistry*
  • S-Adenosylmethionine / metabolism

Substances

  • Iron-Sulfur Proteins
  • S-Adenosylmethionine
  • Acetyltransferases
  • pyruvate formate-lyase activating enzyme