Journal
ACS CATALYSIS
Volume 13, Issue 13, Pages 8613-8623Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acscatal.3c01158
Keywords
methane; hydroxylation; cytochrome P450; wild-type enzyme; decoy molecule; biocatalysis
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This study reports the catalytic oxidation of methane to methanol by wild-type P450BM3 without mutagenesis. The findings have significant implications for the development of biological methane oxidation technology.
Biological methane oxidation is a highly desirable methodfor theconversion of natural gas into a liquid to meet the increasing demandfor fuel and chemical feedstock as well as reducing the potent greenhouseeffects of methane emissions. Because natural hemoenzymes that cancatalyze the conversion of methane to methanol have not been found,it has long been considered that hemoenzymes, including cytochromeP450s (P450s), cannot catalyze the oxidative conversion of methane.Herein, we report the catalytic oxidation of methane by wild-typeP450BM3, without any mutagenesis, in the presence of chemically evolveddummy substrates (decoy molecules) under high-pressure methane at10 MPa. Our studies showed that methane was catalytically convertedinto methanol at room temperature with a total turnover number of4.
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