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, McCormick, Michael S., Behan, Rachel K., Sazinsky, Matthew H., Jiang, Wei, Lin, Jeffery, Krebs, Carsten, Lippard, Stephen J.
Other Authors: Massachusetts Institute of Technology. Department of Chemistry
Format: Article
Language:en_US
Published: American Chemical Society 2011
Online Access:http://hdl.handle.net/1721.1/67685

Internet

http://hdl.handle.net/1721.1/67685

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