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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Veröffentlicht in:	Journal of the American Chemical Society 2010-10, Vol.132 (39), p.13582-13585
Hauptverfasser:	Song, Woon Ju, McCormick, Michael S., Behan, Rachel K., Sazinsky, Matthew H., Jiang, Wei, Lin, Jeffery, Krebs, Carsten, Lippard, Stephen J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Catalytic Domain Crystallography, X-Ray Ferric Compounds - chemistry Ferric Compounds - metabolism Kinetics Models, Molecular Mutagenesis, Site-Directed Oxygen - chemistry Oxygenases - chemistry Oxygenases - genetics Oxygenases - metabolism Protons Threonine - chemistry Threonine - metabolism
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