Active Site Threonine Facilitates Proton Transfer during Dioxygen Activation at the Diiron Center of Toluene/o-Xylene Monooxygenase Hydroxylase

Active Site Threonine Facilitates Proton Transfer during Dioxygen Activation at the Diiron Center of Toluene/o-Xylene Monooxygenase Hydroxylase

Toluene/o-xylene monooxygenase hydroxylase (ToMOH), a diiron-containing enzyme, can activate dioxygen to oxidize aromatic substrates. To elucidate the role of a strictly conserved T201 residue during dioxygen activation of the enzyme, T201S, T201G, T201C, and T201V variants of ToMOH were prepared by...

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Bibliographic Details
Main Authors: Song, Woon Ju (Contributor), McCormick, Michael S. (Contributor), Behan, Rachel K. (Contributor), Sazinsky, Matthew H. (Author), Jiang, Wei (Author), Lin, Jeffery (Author), Krebs, Carsten (Author), Lippard, Stephen J. (Contributor)
Other Authors: Massachusetts Institute of Technology. Department of Chemistry (Contributor)
Format: Article
Language:English
Published: American Chemical Society, 2011-12-14T21:17:05Z.
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