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A promiscuous cytochrome P450 aromatic O-demethylase for lignin bioconversion

DOI: 10.1038/s41467-018-04878-2 DOI Help

Authors: Sam J. B. Mallinson (University of Portsmouth) , Melodie M. Machovina (National Renewable Energy Laboratory; Montana State University) , Rodrigo L. Silveira (National Renewable Energy Laboratory; University of Campinas) , Marc Garcia-borrĂ s (University of California at Los Angeles) , Nathan Gallup (National Renewable Energy Laboratory; University of California at Los Angeles) , 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)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 9

State: Published (Approved)
Published: June 2018

Open Access Open Access

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.

Journal Keywords: Biophysical chemistry; Enzyme mechanisms; Enzymes; Multienzyme complexes; X-ray crystallography

Subject Areas: Biology and Bio-materials


Instruments: I03-Macromolecular Crystallography , I04-Macromolecular Crystallography

Documents:
s41467-018-04878-2.pdf