A Trp199Glu MauG variant reveals a role for Trp199 interactions with pre-methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesis

FEBS Lett. 2013 Jun 19;587(12):1736-41. doi: 10.1016/j.febslet.2013.04.047. Epub 2013 May 10.

Abstract

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Benzoquinones / metabolism
  • Electron Transport
  • Enzyme Precursors / metabolism*
  • Indolequinones / biosynthesis*
  • Iron / metabolism
  • Models, Molecular
  • Mutagenesis, Site-Directed*
  • Mutation*
  • Oxidoreductases Acting on CH-NH Group Donors / chemistry
  • Oxidoreductases Acting on CH-NH Group Donors / metabolism*
  • Paracoccus denitrificans / enzymology
  • Protein Binding
  • Protein Conformation
  • Tryptophan / analogs & derivatives*
  • Tryptophan / biosynthesis
  • Tryptophan / metabolism*

Substances

  • Bacterial Proteins
  • Benzoquinones
  • Enzyme Precursors
  • Indolequinones
  • tryptophan tryptophylquinone
  • quinone
  • Tryptophan
  • Iron
  • methylamine dehydrogenase
  • Oxidoreductases Acting on CH-NH Group Donors