Monday, October 31, 2011, 11:00 am — John Dunn Seminar Room, Bldg. 463
Methylamine dehydrogenase (MADH), a metabolic enzyme found in methylotrophic/autotrophic bacteria, contains a quinone cofactor, tryptophan tryptophylquinone (TTQ), derived from the post-translational modification of two Trp residues in the protein. MauG is a highly unusual c-type di heme enzyme responsible for the completion of TTQ synthesis. The natural substrate for MauG (preMADH) is a 119-kDa protein precursor of MADH with a partially formed cofactor. MauG catalyzes a six-electron oxidation to complete TTQ biosynthesis, using either hydrogen peroxide or oxygen (with reducing equivalents) as the second substrate. The activation of molecular oxygen is highly unusual for a c-type heme system, and crystals of the MauG-preMADH complex support TTQ formation. The catalysis occurs via long-range electron transfer as the oxygen-binding heme is ~ 40 Å from the site of TTQ synthesis. Using X-ray crystallography, single crystal spectroscopy, site-directed mutagenesis and mass spectrometry, this presentation will focus on our latest unpublished in crystallo work.
Hosted by: Allen Orville
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