A promiscuous cytochrome P450 aromatic O-demethylase for lignin bioconversion

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 () and John E. McGeehan ()
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Sam J. B. Mallinson: University of Portsmouth
Melodie M. Machovina: National Renewable Energy Laboratory
Rodrigo L. Silveira: National Renewable Energy Laboratory
Marc Garcia-Borràs: University of California at Los Angeles
Nathan Gallup: National Renewable Energy Laboratory
Christopher W. Johnson: National Renewable Energy Laboratory
Mark D. Allen: University of Portsmouth
Munir S. Skaf: University of Campinas
Michael F. Crowley: National Renewable Energy Laboratory
Ellen L. Neidle: University of Georgia
Kendall N. Houk: University of California at Los Angeles
Gregg T. Beckham: National Renewable Energy Laboratory
Jennifer L. DuBois: Montana State University
John E. McGeehan: University of Portsmouth

Nature Communications, 2018, vol. 9, issue 1, 1-12

Abstract: Abstract 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.

Date: 2018
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DOI: 10.1038/s41467-018-04878-2

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