Journal
CHEMISTRY-A EUROPEAN JOURNAL
Volume 26, Issue 57, Pages 13093-13102Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.202002203
Keywords
cyclization; density functional calculations; enzyme mechanisms; hydroxylation; reaction mechanisms
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Funding
- Punjab Education Endowment Fund (PEEF) in Pakistan
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A recently characterized cytochrome P450 isozyme GcoA activates lignin components through a selectiveO-demethylation or alternatively an acetal formation reaction. These are important reactions in biotechnology and, because lignin is readily available; it being the main component in plant cell walls. In this work we present a density functional theory study on a large active site model of GcoA to investigate syringol activation by an iron(IV)-oxo heme cation radical oxidant (Compound I) leading to hemiacetal and acetal products. Several substrate-binding positions were tested and full energy landscapes calculated. The study shows that substrate positioning determines the product distributions. Thus, with the phenol group pointing away from the heme, anO-demethylation is predicted, whereas an initial hydrogen-atom abstraction of the weak phenolic O-H group would trigger a pathway leading to ring-closure to form acetal products. Predictions on how to engineer P450 GcoA to get more selective product distributions are given.
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