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Author Notes:

Author correspondence: Stephen J. Lippard (Email: lippard@mit.edu) and Boi Hanh Huynh (Email: vhuynh@physics.emory.edu)

We thank Prof. J. Stubbe for use of her freeze-quench apparatus and Dr. L. J. Murray for helpful comments on the manuscript.


Research Funding:

This work was supported by grants GM32134 (to SJL) and GM 47295 (to BHH) from the National Institute of General Medical Sciences.

RKB acknowledges fellowship support from the NIGMS (1 F32 GM084564-01).

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


Journal Title:

Journal of the American Chemical Society


Volume 131, Number 17


, Pages 6074-6075

Type of Work:

Article | Post-print: After Peer Review


We report the observation of a novel intermediate in the reaction of a reduced toluene/o-xylene monooxygenase hydroxylase (ToMOHred) 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 Mössbauer spectroscopic properties of the intermediate allowing us to assign it as a peroxodiiron(III) species, T201Speroxo, similar to Hperoxo in methane monooxygenase. Although T201S generates T201Speroxo in addition to optically transparent ToMOHperoxo, 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.

Copyright information:

© 2009 American Chemical Society

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