ArticleBiochemistry2011
Multiple roles of component proteins in bacterial multicomponent monooxygenases: phenol hydroxylase and toluene/o-xylene monooxygenase from Pseudomonas sp. OX1.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 35 citations in OpenAlex.
- Aniline Degradation via 2-Aminophenol: Genetic Basis, Broadened Players and Interspecies Cooperation.Environmental microbiology · 2026Article
- The Factors Governing Metal Dependence of an Emergent Superfamily of Bimetallic Oxygenases.Journal of the American Chemical Society · 2026Article
- Comparative Genomic Analysis and BTEX Degradation Pathways of a ThermotolerantJournal of microbiology and biotechnology · 2023Article
- A Multicomponent THF Hydroxylase Initiates Tetrahydrofuran Degradation inApplied and environmental microbiology · 2022Article
- Pathways of 4-Hydroxy-2-Nonenal Detoxification in a Human Astrocytoma Cell Line.Antioxidants (Basel, Switzerland) · 2020Article
- Half-of-the-Sites Reactivity of the Castor Δ9-18:0-Acyl Carrier Protein Desaturase.Plant physiology · 2015Article
- Structural basis for biomolecular recognition in overlapping binding sites in a diiron enzyme system.Nature communications · 2014Article
- Electron transfer control in soluble methane monooxygenase.Journal of the American Chemical Society · 2014Article
- A flexible glutamine regulates the catalytic activity of toluene o-xylene monooxygenase.Biochemistry · 2014Article
- Cyanobacterial aldehyde deformylase oxygenation of aldehydes yields n-1 aldehydes and alcohols in addition to alkanes.ACS catalysis · 2013Article
- Hydroquinone: environmental pollution, toxicity, and microbial answers.BioMed research international · 2013Review
- Article
- Mechanistic studies of reactions of peroxodiiron(III) intermediates in T201 variants of toluene/o-xylene monooxygenase hydroxylase.Biochemistry · 2011Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Phenol hydroxylase (PH) and toluene/o-xylene monooxygenase (ToMO) from Pseudomonas sp. OX1 require three or four protein components to activate dioxygen for the oxidation of aromatic substrates at a carboxylate-bridged diiron center. In this study, we investigated the influence of the hydroxylases, regulatory proteins, and electron-transfer components of these systems on substrate (phenol; NADH) consumption and product (catechol; H(2)O(2)) generation. Single-turnover experiments revealed that only complete systems containing all three or four protein components are capable of oxidizing phenol, a major substrate for both enzymes. Under ideal conditions, the hydroxylated product yield was ∼50% of the diiron centers for both systems, suggesting that these enzymes operate by half-sites reactivity mechanisms. Single-turnover studies indicated that the PH and ToMO electron-transfer components exert regulatory effects on substrate oxidation processes taking place at the hydroxylase actives sites, most likely through allostery. Steady state NADH consumption assays showed that the regulatory proteins facilitate the electron-transfer step in the hydrocarbon oxidation cycle in the absence of phenol. Under these conditions, electron consumption is coupled to H(2)O(2) formation in a hydroxylase-dependent manner. Mechanistic implications of these results are discussed.
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