A promiscuous cytochrome P450 aromatic O-demethylase for lignin bioconversion
Research output: Contribution to journal › Article › peer-review
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 | English |
---|---|
Article number | 2487 |
Journal | Nature Communications |
Volume | 9 |
Issue number | 1 |
DOIs | |
Publication status | Published - 27 Jun 2018 |
Documents
- A promiscuous cytochrome P450
Final published version, 2.1 MB, PDF document
Licence: CC BY
Links
Related information
Media
A new enzyme that will 'eat' plastic pollution
Press/Media: Research
ID: 8499664