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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

A promiscuous cytochrome P450 aromatic O-demethylase for lignin bioconversion

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Mallinson, Sam J. B. [1] ; Machovina, Melodie M. [2, 3] ; Silveira, Rodrigo L. [4, 3] ; Garcia-Borras, Marc [5] ; Gallup, Nathan [5, 3] ; Johnson, Christopher W. [3] ; Allen, Mark D. [1] ; Skaf, Munir S. [4] ; Crowley, Michael F. [6] ; Neidle, Ellen L. [7] ; Houk, Kendall N. [5] ; Beckham, Gregg T. [3] ; DuBois, Jennifer L. [2] ; McGeehan, John E. [1]
Total Authors: 14
[1] Univ Portsmouth, Sch Biol Sci, Inst Biol & Biomed Sci, Mol Biophys, Portsmouth PO1 2DY, Hants - England
[2] Montana State Univ, Dept Chem & Biochem, Bozeman, MT 59717 - USA
[3] Natl Bioenergy Ctr, Natl Renewable Energy Lab, Golden, CO 80401 - USA
[4] Univ Estadual Campinas, Inst Chem, BR-13083970 Campinas, SP - Brazil
[5] Univ Calif Los Angeles, Dept Chem & Biochem, Los Angeles, CA 90095 - USA
[6] Biosci Ctr, Natl Renewable Energy Lab, Golden, CO 80401 - USA
[7] Univ Georgia, Dept Microbiol, Athens, GA 30602 - USA
Total Affiliations: 7
Document type: Journal article
Source: NATURE COMMUNICATIONS; v. 9, JUN 27 2018.
Web of Science Citations: 23

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. (AU)

FAPESP's process: 13/08293-7 - CCES - Center for Computational Engineering and Sciences
Grantee:Munir Salomao Skaf
Support type: Research Grants - Research, Innovation and Dissemination Centers - RIDC
FAPESP's process: 14/10448-1 - Molecular aspects of plant cell wall architecture
Grantee:Rodrigo Leandro Silveira
Support type: Scholarships in Brazil - Post-Doctorate
FAPESP's process: 16/22956-7 - Hybrid QM/MM simulations of feruloyl esterases: cleavage mechanism of lignin-carbohydrate complexes in plant cell walls
Grantee:Rodrigo Leandro Silveira
Support type: Scholarships abroad - Research Internship - Post-doctor