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


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.

SUBMITTER: Cooke HA 

PROVIDER: S-EPMC3458437 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature

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

Cooke Heather A HA   Peck Spencer C SC   Evans Bradley S BS   van der Donk Wilfred A WA  

Journal of the American Chemical Society 20120913 38


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 me  ...[more]

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