Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Kinetics of proton-linked flavin conformational changes in p-hydroxybenzoate hydroxylase.

Biochemistry - 11 Oct 2005

Frederick Kendra King, Palfey Bruce A

Abstract excerpt

p-Hydroxybenzoate hydroxylase (PHBH) is an FAD-dependent monooxygenase that catalyzes the hydroxylation of p-hydroxybenzoate (pOHB) to 3,4-dihydroxybenzoate in an NADPH-dependent reaction. Two structural features are coupled to control the reactivity of PHBH with NADPH: a proton-transfer network that allows protons to be passed between the sequestered active site and solvent and a flavin that adopts two...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Catalysis
Share to Flavins
Share to Fluorescent Dyes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mixed Function Oxygenases

Share to Models, Chemical

Share to Protons

Share to Pseudomonas aeruginosa

Source

Identifiers

PMID: 16201756
DOI: 10.1021/bi051119t

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Kinetics of proton-linked flavin conformational changes in p-hydroxybenzoate hydroxylase.PMID 16201756Read ↗

Protein dynamics and electrostatics in the function of p-hydroxybenzoate hydroxylase.Semantic proximity Read ↗

Crystal structures of wild-type p-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate,2,4-dihydroxybenzoate, and 2-hydroxy-4-aminobenzoate and of the Tyr222Ala mutant complexed with 2-hydroxy-4-aminobenzoate. Evidence for a proton channel and a new binding mode of the flavin ring.Semantic proximity Read ↗

Mechanistic insights into p-hydroxybenzoate hydroxylase from studies of the mutant Ser212Ala.Semantic proximity Read ↗

Evidence for flavin movement in the function of p-hydroxybenzoate hydroxylase from studies of the mutant Arg220Lys.Semantic proximity Read ↗

Catalytic efficiency of enzymes: a theoretical analysis.Semantic proximity Read ↗

Properties of p-hydroxybenzoate hydroxylase when stabilized in its open conformation.Semantic proximity Read ↗

The effect of a Glu370Asp mutation in glutaryl-CoA dehydrogenase on proton transfer to the dienolate intermediate.Semantic proximity Read ↗

Kinetic isotope effects on the noncovalent flavin mutant protein of pyranose 2-oxidase reveal insights into the flavin reduction mechanism.Semantic proximity Read ↗

Control of C4a-hydroperoxyflavin protonation in the oxygenase component of p-hydroxyphenylacetate-3-hydroxylase.Semantic proximity Read ↗

A Single-Site Mutation at Ser146 Expands the Reactivity of the Oxygenase Component of p-Hydroxyphenylacetate 3-Hydroxylase.Semantic proximity Read ↗

Kinetic and isotopic characterization of L-proline dehydrogenase from Mycobacterium tuberculosis.Semantic proximity Read ↗

Distance variations between active sites of H(+)-pyrophosphatase determined by fluorescence resonance energy transfer.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.