MauG-dependent in vitro biosynthesis of tryptophan tryptophylquinone in methylamine dehydrogenase

Yongting Wang, Xianghui Li, Limei H. Jones, Arwen R. Pearson, Carrie M. Wilmot, Victor L. Davidson

Research output: Contribution to journalArticlepeer-review

49 Scopus citations


Tryptophan tryptophylquinone (TTQ) is the prosthetic group of methylamine dehydrogenase (MADH) and is synthesized through post-translational modification of two endogenous tryptophan residues. This modification involves two oxygenation reactions and one cross-linking reaction. It is clearly shown that the incorporation of the second oxygen into βTrp 57 and the covalent cross-linking of βTrp 57 to βTrp 108 are MauG-dependent processes. These reaction steps are severely compromised in vivo when mauG is mutated or deleted. These steps may then be catalyzed in vitro upon addition of MauG to the isolated biosynthetic intermediates. These results also show that TTQ formation is linked to proper assembly of subunits during MADH biosynthesis. Last, these results demonstrate a novel function for the c-type heme protein, MauG, which is consistent with its atypical physical properties. These results are the first description of an enzyme-mediated biosynthesis of a protein-derived cofactor in vitro.

Original languageEnglish (US)
Pages (from-to)8258-8259
Number of pages2
JournalJournal of the American Chemical Society
Issue number23
StatePublished - Jun 15 2005


Dive into the research topics of 'MauG-dependent in vitro biosynthesis of tryptophan tryptophylquinone in methylamine dehydrogenase'. Together they form a unique fingerprint.

Cite this