Carboxyl group of Glu113 is required for stabilization of the diferrous and bis-Fe(IV) states of MauG

The diheme enzyme MauG catalyzes a six-electron oxidation required for post-translational modification of a precursor of methylamine dehydrogenase (preMADH) to complete the biosynthesis of its protein-derived tryptophan tryptophylquinone (TTQ) cofactor. Crystallographic studies have implicated Glu11...

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Veröffentlicht in:	Biochemistry (Easton) 2013-09, Vol.52 (37), p.6358
Hauptverfasser:	Abu Tarboush, Nafez, Yukl, Erik T, Shin, Sooim, Feng, Manliang, Wilmot, Carrie M, Davidson, Victor L
Format:	Artikel
Sprache:	eng
Schlagworte:	Crystallography, X-Ray Ferric Compounds - chemistry Ferrous Compounds - chemistry Glutamic Acid - chemistry Heme - chemistry Hemeproteins - chemistry Hydrogen Peroxide Indolequinones - biosynthesis Oxidation-Reduction Oxidoreductases Acting on CH-NH Group Donors - chemistry Oxidoreductases Acting on CH-NH Group Donors - metabolism Paracoccus denitrificans - enzymology Protein Processing, Post-Translational Tryptophan - analogs & derivatives Tryptophan - biosynthesis
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