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Characterization of a Peroxodiiron(III) Intermediate in the T201S Variant of Toluene/<i>o</i>-Xylene Monooxygenase Hydroxylase from <i>Pseudomonas</i> sp OX1

Cited 30 time in Web of Science Cited 33 time in Scopus
Authors

Song, Woon Ju; Behan, Rachel K.; Naik, Sunil G.; Huynh, Boi Hanh; Lippard, Stephen J.

Issue Date
2009-05
Publisher
AMER CHEMICAL SOC
Citation
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, Vol.131 No.17, pp.6074-+
Abstract
We report the observation of a novel intermediate in the reaction of a reduced toluene/o-xylene monooxygenase hydroxylase (ToMOH(red)) T201S variant, in the presence of a regulatory protein (ToMOD), with dioxygen. This species is the first oxygenated intermediate with an optical band in any toluene monooxygenase. The UV-vis and Mossbauer spectroscopic properties of the intermediate allow us to assign it as a peroxodiiron(III) species, T201S(peroxo), similar to H-peroxo in methane monooxygenase. Although T201S generates T201S(peroxo) in addition to optically transparent ToMOH(peroxo), previously observed in wild-type ToMOH, this conservative variant is catalytically active in steady-state catalysis and single-turnover experiments and displays the same regiospecificity for toluene and slightly different regiospecificity for o-xylene oxidation.
ISSN
0002-7863
URI
https://hdl.handle.net/10371/203495
DOI
https://doi.org/10.1021/ja9011782
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  • College of Natural Sciences
  • Department of Chemistry
Research Area Biochemistry, Inorganic, 무기화학, 생화학

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