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Extensive hydrolysis of phosphonates as unexpected behaviour of the known His6-organophosphorus hydrolase.

Ilya V LyaginMariia S AndrianovaElena N Efremenko
Published in: Applied microbiology and biotechnology (2016)
The catalytic activity of hexahistidine-tagged organophosphorus hydrolase (His6-OPH) in hydrolytic reactions of methylphosphonic acid (MPA) and its monoesters and diesters being decomposition products of R-VX was demonstrated for the first time. The catalytic constants of enzyme in such reactions were determined. The mechanism of C-P bond cleavage in the MPA by His6-OPH was proposed. Such reaction was estimated to be carried out with the soluble and nanocapsulated forms of His6-OPH. His6-OPH was demonstrated to be capable of degrading the key organophosphorus components of reaction masses (RMs) that are produced by the chemical detoxification of R-VX and RMs are multi-substrate mixtures for this enzyme. The kinetic model describing the behaviour of His6-OPH in RMs was proposed and was shown to adequately fit experimental points during degradation of the real samples of RMs.
Keyphrases
  • magnetic resonance imaging
  • ionic liquid
  • electron transfer
  • amino acid
  • anaerobic digestion