Isotope labeling studies reveal the order of oxygen incorporation into the tryptophan tryptophylquinone cofactor of methylamine dehydrogenase

Arwen R. Pearson, Sudha Marimanikkuppam, Xianghui Li, Victor L. Davidson, Carrie M. Wilmot

Research output: Contribution to journalArticle

18 Scopus citations

Abstract

The bacterial enzyme methylamine dehydrogenase (MADH) contains the protein-derived cofactor tryptophan tryptophylquinone (TTQ). TTQ is generated by the posttranslational modification of two endogenous MADH tryptophans, βW57 and βW108. Two oxygens are inserted sequentially into βW57 to generate the quinone moiety, after which it is cross-linked to βW108. We have previously shown that the second oxygenation and cross-link formation are catalyzed by the novel di-heme cytochrome MauG. Here we show, using isotopically labeled oxygen and water, that the first addition of oxygen occurs specifically at the C7 position of βW57 and that MauG then inserts the second oxygen at position C6.

Original languageEnglish (US)
Pages (from-to)12416-12417
Number of pages2
JournalJournal of the American Chemical Society
Volume128
Issue number38
DOIs
StatePublished - Sep 27 2006

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