Crystal structures of CO and NO adducts of MauG in complex with pre-methylamine dehydrogenase: implications for the mechanism of dioxygen activation.

Abstract

MauG is a diheme enzyme responsible for the post-translational formation of the catalytic tryptophan tryptophylquinone (TTQ) cofactor in methylamine dehydrogenase (MADH). MauG can utilize hydrogen peroxide, or molecular oxygen and reducing equivalents, to complete this reaction via a catalytic bis-Fe(IV) intermediate. Crystal structures of diferrous, Fe(II… (More)
DOI: 10.1021/bi200023n

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@article{Yukl2011CrystalSO, title={Crystal structures of CO and NO adducts of MauG in complex with pre-methylamine dehydrogenase: implications for the mechanism of dioxygen activation.}, author={Erik T Yukl and Brandon R. Goblirsch and Victor L Davidson and Carrie M Wilmot}, journal={Biochemistry}, year={2011}, volume={50 14}, pages={2931-8} }