Researchers reveal novel mechanism of enhanced P450 demethylase activity through engineered key gating residues

Researchers have developed a novel mechanism to enhance the activity of P450 demethylase, crucial for lignin degradation, by engineering key gating residues. The team transformed CYP199A4, which typically depends on NADH, into a peroxygenase that utilizes H₂O₂. They created mutant libraries to study lignin analogs, achieving impressive conversion rates. Structural analysis and simulations showed reduced barriers for H₂O₂ access, improving efficiency. This advancement in P450 peroxygenases could significantly impact synthetic chemistry and biology.

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