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Publication Abstract from PubMed

Hydroxylation of phenols into polyphenols, valuable chemical and pharmaceutical products, is a challenging reaction. The search for green synthetic processes has led to considering microorganisms as well as pure hydroxylases as catalysts for phenol hydroxylation. Here we report the structural and functional characterization of the FAD-dependent 4-hydroxyphenylacetate 3-monooxygenase from Escherichia coli, named HpaB. We show that this enzyme enjoys a relatively broad substrate specificity, allowing conversion of a number of non-natural phenolic compounds such as tyrosol, hydroxymandelic acid, coumaric acid, hydroxybenzoic acid and its methyl ester and phenol into the corresponding catechols. The reaction can be carried out using a simple chemical assay based on formate as the electron donor and the organometallic complex [Cp*Rh(bpy)(H2O)]2+ as the catalyst for FAD reduction. The availability of a crystal structure of HpaB in complex with FAD 1.8 A resolution opens the possibility of rational tuning of the substrate specificity and the activity of this interesting class of phenol hydroxylases.

Structure and functional characterization of 4-hydroxyphenylacetate 3-hydroxylase from Escherichia coli.,Deng Y, Faivre B, Back O, Lombard M, Pecqueur L, Fontecave M Chembiochem. 2019 Jun 2. doi: 10.1002/cbic.201900277. PMID:31155821^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.