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Showing 1 to 6 of 6 for “"phenol hydroxylase"”.
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Characterisation of phenol hydroxylase and its auxiliary proteins, DmpM and DmpK, from pseudomonas spl Strain CF600
Phenol hydroxylase from Pseudomonas sp. strain CF600 is an enzyme comprising three components: DmpP, a reductase containing an FAD and a [2Fe-2S] cluster; DmpM, an activator protein required for efficient catalysis; and DmpLNO, an oxygenase containing a binuclear iron cluster. The oxygenase …
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Rekombinante Herstellung und Charakterisierung phenoloxidierender Enzyme aus Geobacillus stearothermophilus zur Evaluierung einer biosensorischen Anwendung
… the current thesis the genetic structure of the phenol hydroxylase of Geobacillus stearothermophilus has been clarified. The single components Phe A1 (oxygenase component), Phe A2 (Flavin reductase component) and a tandem construct consisting of both components were successfully produced with an …
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Dioxygen activation and substrate hydroxylation by the hydroxylase component of toluene/O-xylene monooxygenase from pseudomonas sporium OX1
… carboxylate-bridged diiron centers in the hydroxylase components of the bacterial multicomponent monooxygenases activate dioxygen at structurally homologous active sites. Catalysis requires the management of four substrates: electrons, protons, dioxygen, and hydrocarbons. Protein component …
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Structural investigations of hydroxylase proteins and complexes in bacterial multicomponent monooxygenase systems
… such as toluene/o-xylene monooxygenase (ToMO), phenol hydroxylase (PH), and soluble methane monooxygenase (sMMO) catalyze hydrocarbon oxidation reactions at a carboxylatebridged non-heme diiron center common to many systems in biology, as discussed in the first and subsequent chapters of this …
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Exploring reactivity and component interactions in Toluene/o-Xylene Monooxygenase from pseudomonas sp. OX1
… a diiron active site housed within a catalytic hydroxylase protein. This diiron active site is responsible for activation of dioxygen and oxidation of hydrocarbons. Additional component proteins modify the structure of the hydroxylase regulating substrate access and pre-organizing the diiron …
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Exploring the reactivity of bacterial multicomponent monooxygenases
… Performed by Soluble Methane Monooxygenase Hydroxylase Intermediates Hroxo and Q Proceed by Distinct Mechanisms Soluble methane monooxygenase is a bacterial enzyme that converts methane to methanol at a carboxylate-bridged diiron center with exquisite control. Because the oxidizing power …