Mechanistic investigation of methylphosphonate synthase, a non-heme iron-dependent oxygenase

Heather A. Cooke, Spencer C. Peck, Bradley S. Evans, Wilfred A. Van Der Donk

Research output: Contribution to journalArticlepeer-review


Methylphosphonate synthase is a non-heme iron-dependent oxygenase that converts 2-hydroxyethylphosphonate (2-HEP) to methylphosphonate. On the basis of experiments with two enantiomers of a substrate analog, 2- hydroxypropylphosphonate, catalysis is proposed to commence with stereospecific abstraction of the pro-S hydrogen on C2 of the substrate. Experiments with isotopologues of 2-HEP indicate stereospecific hydrogen transfer of the pro-R hydrogen at C2 of the substrate to the methyl group of methylphosphonate. Kinetic studies with these substrate isotopologues reveal that neither hydrogen transfer is rate limiting under saturating substrate conditions. A mechanism is proposed that is consistent with the available data.

Original languageEnglish (US)
Pages (from-to)15660-15663
Number of pages4
JournalJournal of the American Chemical Society
Issue number38
StatePublished - Sep 26 2012

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry


Dive into the research topics of 'Mechanistic investigation of methylphosphonate synthase, a non-heme iron-dependent oxygenase'. Together they form a unique fingerprint.

Cite this