期刊
NATURE COMMUNICATIONS
卷 9, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-018-04878-2
关键词
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资金
- NSF [MCB-1715176, CHE-1361104, DEB-1556541, MCB-1615365]
- BBSRC [BB/P011918/1, BB/L001926/1]
- U.S. Department of Energy Energy Efficiency and Renewable Energy Bioenergy Technologies Office (DOE EERE BETO) [DE-AC36-08GO28308]
- National Renewable Energy Laboratory [DE-AC36-08GO28308]
- U.S. Department of Energy, Office of Science, Office of Workforce Development for Teachers and Scientists, Office of Science Graduate Student Research (SCGSR) program
- DOE [DE-SC0014664]
- Sao Paulo Research Foundation
- Center for Computational Engineering and Sciences [2013/08293-7, 2014/10448-1, 2016/22956-7]
- Ramon Areces Foundation
- DOE Office of EERE [DE-AC36-08GO28308]
- Direct For Mathematical & Physical Scien [1361104] Funding Source: National Science Foundation
- Division Of Chemistry [1361104] Funding Source: National Science Foundation
- BBSRC [BB/L001926/1, BB/P011918/1] Funding Source: UKRI
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.
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