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A promiscuous cytochrome P450 aromatic O-demethylase for lignin bioconversion

Research output: Contribution to journalArticlepeer-review

  • Sam J. B. Mallinson
  • Melodie M. Machovina
  • Rodrigo L. Silveira
  • Marc Garcia-Borràs
  • Nathan Gallup
  • Christopher W. Johnson
  • Mark D. Allen
  • Munir S. Skaf
  • Michael F. Crowley
  • Ellen L. Neidle
  • Kendall N. Houk
  • Gregg T. Beckham
  • Jennifer L. DuBois
  • Professor John McGeehan
Microbial aromatic catabolism offers a promising approach to convert lignin, a vast source of renewable carbon, into useful products. Aryl-O-demethylation is an essential biochemical reaction to ultimately catabolize coniferyl and sinapyl lignin-derived aromatic compounds, and is often a key bottleneck for both native and engineered bioconversion pathways. Here, we report the comprehensive characterization of a promiscuous P450 aryl-O-demethylase, consisting of a cytochrome P450 protein from the family CYP255A (GcoA) and a three-domain reductase (GcoB) that together represent a new two-component P450 class. Though originally described as converting guaiacol to catechol, we show that this system efficiently demethylates both guaiacol and an unexpectedly wide variety of lignin-relevant monomers. Structural, biochemical, and computational studies of this novel two-component system elucidate the mechanism of its broad substrate specificity, presenting it as a new tool for a critical step in biological lignin conversion.
Original languageEnglish
Article number2487
JournalNature Communications
Issue number1
Publication statusPublished - 27 Jun 2018


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