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.
Original language | American English |
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Article number | 2487 |
Number of pages | 12 |
Journal | Nature Communications |
Volume | 9 |
Issue number | 1 |
DOIs | |
State | Published - 1 Dec 2018 |
Bibliographical note
Publisher Copyright:© 2018 The Author(s).
NREL Publication Number
- NREL/JA-5100-71206
Keywords
- enzyme characterization
- enzyme discovery
- lignin conversion
- protein family