A Trp199Glu MauG variant reveals a role for Trp199 interactions with pre-methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesis
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- 作者：Nafez Abu Tarboush ; Lyndal M.R. Jensen ; Carrie M. Wilmot ; Victor L. Davidson
- 关键词：Em ; Oxidation&ndash ; reduction midpoint potential ; ET ; electron transfer ; MADH ; methylamine dehydrogenase ; TTQ ; tryptophan tryptophylquinone ; preMADH ; the biosynthetic precursor protein of MADH with incompletely synthesized TTQ ; WT ; wild-type
- 刊名：FEBS Letters
- 出版年：2013
- 出版时间：19 June, 2013
- 年：2013
- 卷：587
- 期：12
- 页码：1736-1741
- 全文大小：1216 K
文摘
MauG catalyzes posttranslational modifications of a methylamine dehydrogenase precursor (preMADH) to complete the biosynthesis of its protein-derived tryptophan tryptophylquinone (TTQ) cofactor. Trp199 is present at the site of interaction between MauG and preMADH and is critical to this process as it mediates hole hopping during the inter-protein electron transfer that is required for catalysis. Trp199 was converted to Glu and the structure and reactivity of the W199E/preMADH complex were characterized. The results reveal that the nature of residue 199 is also important for productive complex formation between preMADH and MauG.