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- W793412565 abstract "An intriguing mystery about tryptophan 2, 3-dioxygenase is its hydrogen peroxide-triggered enzyme reactivation from the resting ferric oxidation state to the catalytically active ferrous form. In this study, we found that such an odd Fe(III) reduction by an oxidant depends on the presence of L-Trp, which ultimately serves as the reductant for the enzyme. In the peroxide reaction with tryptophan 2, 3-dioxygenase, a previously unknown catalase-like activity was detected. A ferryl species (δ = 0.055 mm/s and ΔEQ = 1.755 mm/s) and a protein-based free radical (g = 2.0028 and 1.72 millitesla linewidth) were characterized by Mossbauer and EPR spectroscopy, respectively. This is the first compound ES-type of ferryl intermediate from a heme-based dioxygenase characterized by EPR and Mossbauer spectroscopy. Density functional theory calculations revealed the contribution of secondary ligand sphere to the spectroscopic properties of the ferryl species. A Trp-Trp dimer and a monooxygenated L-Trp were both observed as the enzyme reactivation by-products by mass spectrometry. Together, these results lead to the unraveling of an over 60-year old mystery of peroxide reactivation mechanism. INDEX WORDS: Tryptophan dioxygenase, Radical, Methylamine dehydrogenase, Electron paramagnetic spectroscopy, Mossbauer spectroscopy, INTERACTIONS OF METALS AND RADICALS: A BIOCHEMICAL PERSPECTIVE IN TRYPTOPHAN DIOXYGENASE" @default.
- W793412565 created "2016-06-24" @default.
- W793412565 creator A5076148265 @default.
- W793412565 date "2011-01-01" @default.
- W793412565 modified "2023-09-26" @default.
- W793412565 title "Interactions of Metals and Radicals: A Biochemical Perspective in Tryptophan Dioxygenase" @default.
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