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Article

Properties of p-hydroxybenzoate hydroxylase when stabilized in its open conformation.

Biochemistry - 15 Nov 2005

Cole Lindsay J, Entsch Barrie, Ortiz-Maldonado Mariliz, Ballou David P

Abstract excerpt

p-Hydroxybenzoate hydroxylase is extensively studied as a model for single-component flavoprotein monooxygenases. It catalyzes a reaction in two parts: (1) reduction of the FAD in the enzyme by NADPH in response to binding of p-hydroxybenzoate to the enzyme and (2) oxidation of reduced FAD with oxygen in an environment free from solvent to form a hydroperoxide, which then reacts with p-hydroxybenzoate to form an...

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PMID: 16274228
DOI: 10.1021/bi0512142

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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