Single Turnover Reveals Oxygenated Intermediates in Toluene/o-Xylene Monooxygenase in the Presence of the Native Redox Partners
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Author(s)
Liang, Alexandria D
Lippard, Stephen J.
Date Issued
August 2015
Journal
Journal of the American Chemical Society
Publisher
American Chemical Society (ACS)
Citation
Liang, Alexandria Deliz and Lippard, Stephen J. "Single Turnover Reveals Oxygenated Intermediates in Toluene/o-Xylene Monooxygenase in the Presence of the Native Redox Partners." Journal of the American Chemical Society 137, no. 33 (August 2015): 10520–10523 © 2015 American Chemical Society
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Author's final manuscript
Abstract
Toluene/o-xylene monooxygenase (ToMO) is a non-heme diiron protein that activates O₂ for subsequent arene oxidation. ToMO utilizes four protein components, a catalytic hydroxylase, a regulatory protein, a Rieske protein, and a reductase. O₂ activation and substrate hydroxylation in the presence of all four protein components is examined. These studies demonstrate the importance of native reductants by revealing reactivity unobserved when dithionite and mediators are used as the reductant. This reactivity is compared with that of other O₂-activating diiron enzymes.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
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DOI of Published Version
https://doi.org/10.1021/jacs.5b07055
