Work

Mechanistic Investigation of Methylphosphonate Synthase, a Non-Heme Iron-Dependent Oxygenase

Year: 2012

Type: article

Abstract: 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.

Source: Journal of the American Chemical Society

DOI: 10.1021/ja306777w

Authors: Heather A. Cooke, Spencer C. Peck, Bradley S. Evans, Wilfred A. van der Donk

Institutions: Howard Hughes Medical Institute, University of Illinois Urbana-Champaign, Carl R. Woese Institute for Genomic Biology

Language: English

Topic: Metal-Catalyzed Oxygenation Mechanisms

Subfield: Inorganic Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: hybrid

Estimated APC paid: $4,500

Funders: Howard Hughes Medical Institute, National Institutes of Health, National Institute of General Medical Sciences, National Center for Research Resources