ArticleThe Journal of biological chemistry2013
The reaction kinetics of 3-hydroxybenzoate 6-hydroxylase from Rhodococcus jostii RHA1 provide an understanding of the para-hydroxylation enzyme catalytic cycle.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 33 citations in OpenAlex.
- Revealing 3-hydroxybenzoate-4-hydroxylase from Pseudarthrobacter phenanthrenivorans Sphe3 via In-Cell NMR analysis and molecular cloning.International microbiology : the official journal of the Spanish Society for Microbiology · 2026Article
- DFT modeling of water-assisted hydrogen peroxide formation from a C(4a)-(hydro)peroxyflavin.Turkish journal of chemistry · 2024Article
- Identification of a Phylogenetically Divergent Vanillate O-Demethylase fromMicroorganisms · 2022Article
- The role of remote flavin adenine dinucleotide pieces in the oxidative decarboxylation catalyzed by salicylate hydroxylase.Bioorganic chemistry · 2022Article
- Structural and chemical trapping of flavin-oxide intermediates reveals substrate-directed reaction multiplicity.Protein science : a publication of the Protein Society · 2020Article
- Purification and Initial Characterization of 3-Hydroxybenzoate 6-Hydroxylase From a HalophilicFrontiers in microbiology · 2018Article
- Kinetic Mechanism of the Dechlorinating Flavin-dependent Monooxygenase HadA.The Journal of biological chemistry · 2017Article
- 3-Hydroxybenzoate 6-Hydroxylase fromFrontiers in microbiology · 2017Article
- Reaction of pyranose dehydrogenase from Agaricus meleagris with its carbohydrate substrates.The FEBS journal · 2015Article
- Aromatic hydroxylation of salicylic acid and aspirin by human cytochromes P450.European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences · 2015Article
- Mechanism of the 6-hydroxy-3-succinoyl-pyridine 3-monooxygenase flavoprotein from Pseudomonas putida S16.The Journal of biological chemistry · 2014Article
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5 authors at 3 institutions in 2 countries.
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Abstract
3-Hydroxybenzoate 6-hydroxylase (3HB6H) from Rhodococcus jostii RHA1 is an NADH-specific flavoprotein monooxygenase that catalyzes the para-hydroxylation of 3-hydroxybenzoate (3HB) to form 2,5-dihydroxybenzoate (2,5-DHB). Based on results from stopped-flow spectrophotometry, the reduced enzyme-3HB complex reacts with oxygen to form a C4a-peroxy flavin with a rate constant of 1.13 ± 0.01 × 10(6) m(-1) s(-1) (pH 8.0, 4 °C). This intermediate is subsequently protonated to form a C4a-hydroperoxyflavin with a rate constant of 96 ± 3 s(-1). This step shows a solvent kinetic isotope effect of 1.7. Based on rapid-quench measurements, the hydroxylation occurs with a rate constant of 36 ± 2 s(-1). 3HB6H does not exhibit substrate inhibition on the flavin oxidation step, a common characteristic found in most ortho-hydroxylation enzymes. The apparent kcat at saturating concentrations of 3HB, NADH, and oxygen is 6.49 ± 0.02 s(-1). Pre-steady state and steady-state kinetic data were used to construct the catalytic cycle of the reaction. The data indicate that the steps of product release (11.7 s(-1)) and hydroxylation (36 ± 2 s(-1)) partially control the overall turnover.
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