Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinone

Victor L. Davidson, Carrie M. Wilmot

Research output: Contribution to journalReview articlepeer-review

29 Scopus citations

Abstract

Methylamine dehydrogenase (MADH) catalyzes the oxidative deamination of methylamine to formaldehyde and ammonia. Tryptophan tryptophylquinone (TTQ) is the protein-derived cofactor of MADH required for this catalytic activity. TTQ is biosynthesized through the posttranslational modification of two tryptophan residues within MADH, during which the indole rings of two tryptophan side chains are cross-linked and two oxygen atoms are inserted into one of the indole rings. MauG is a c-type diheme enzyme that catalyzes the final three reactions in TTQ formation. In total, this is a six-electron oxidation process requiring three cycles of MauG-dependent two-electron oxidation events using either H2O2 or O2. The MauG redox form responsible for the catalytic activity is an unprecedented bis-FeIV species. The amino acids of MADH that are modified are ∼40 Å from the site where MauG binds oxygen, and the reaction proceeds by a hole hopping electron transfer mechanism. This review addresses these highly unusual aspects of the long-range catalytic reaction mediated by MauG.

Original languageEnglish (US)
Pages (from-to)531-550
Number of pages20
JournalAnnual Review of Biochemistry
Volume82
DOIs
StatePublished - Jun 2013

Keywords

  • Electron transfer
  • Enzyme
  • Heme
  • High-valent iron
  • Hole hopping

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