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Updated: May 22, 2026

Preparation and Use of Carbonyl-decorated Carbenes in the Activation of White Phosphorus
Published on: October 3, 2014
PhnY and PhnZ comprise a new oxidative pathway for enzymatic cleavage of a carbon-phosphorus bond
Fern R McSorley1, Peter B Wyatt, Asuncion Martinez
1Department of Chemistry, Queen's University, Kingston, Ontario, Canada.
Abstract:
The sequential activities of PhnY, an α-ketoglutarate/Fe(II)-dependent dioxygenase, and PhnZ, a Fe(II)-dependent enzyme of the histidine-aspartate motif hydrolase family, cleave the carbon-phosphorus bond of the organophosphonate natural product 2-aminoethylphosphonic acid. PhnY adds a hydroxyl group to the α-carbon, yielding 2-amino-1-hydroxyethylphosphonic acid, which is oxidatively converted by PhnZ to inorganic phosphate and glycine. The PhnZ reaction represents a new enzyme mechanism for metabolic cleavage of a carbon-phosphorus bond.
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