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

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• 作者：Heather A. Cooke ; Spencer C. Peck ; Bradley S. Evans ; Wilfred A. van der Donk
• 刊名：The Journal of the American Chemical Society
• 出版年：2012
• 出版时间：September 26, 2012
• 年：2012
• 卷：134
• 期：38
• 页码：15660-15663
• 全文大小：222K
• 年卷期：v.134,no.38(September 26, 2012)
• ISSN：1520-5126

文摘

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.