Kinetic and isotopic studies of the oxidative half-reaction of phenol hydroxylase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference37 articles.
1. On the Structure of Flavin-Oxygen Intermediates Involved in Enzymatic Reactions
2. Identifications of the true carbon-13 nuclear magnetic resonance spectrum of the stable intermediate II in bacterial luciferase
3. Effect of substrate and pH on the oxidative half-reaction of phenol hydroxylase.
4. p-Hydroxybenzoate Hydroxylase from Pseudomonas fluorescens
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1. Hydrogen movements in the oxidative half-reaction of kynurenine 3-monooxygenase from Pseudomonas fluorescens reveal the mechanism of hydroxylation;Archives of Biochemistry and Biophysics;2020-09
2. Kinetic Mechanisms of the Oxygenase from a Two-component Enzyme, p-Hydroxyphenylacetate 3-Hydroxylase from Acinetobacter baumannii;Journal of Biological Chemistry;2006-06
3. Mechanism of flavin transfer and oxygen activation by the two-component flavoenzyme styrene monooxygenase;Archives of Biochemistry and Biophysics;2005-10
4. Studies on the oxidative half-reaction of p-hydroxyphenylacetate 3-hydroxylase.;Journal of Biological Chemistry;1994-04
5. On the reaction mechanism of phenol hydroxylase. New information obtained by correlation of fluorescence and absorbance stopped flow studies.;Journal of Biological Chemistry;1993-02
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