Reaction of 2-thio-FAD-reconstituted p-hydroxybenzoate hydroxylase with hydrogen peroxide. Formation of a covalent flavin-protein linkage.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference23 articles.
1. Purification and Properties of p-Hydroxybenzoate Hydroxylase from Pseudomonas fluorescens
2. Flavin-oxygen derivatives involved in hydroxylation by p-hydroxybenzoate hydroxylase.
3. Catalytic mechanism of p-hydroxybenzoate hydroxylase with p-mercaptobenzoate as substrate.
4. Fluoride elimination from substrates in hydroxylation reactions catalyzed by p-hydroxybenzoate hydroxylase.
5. Oxygen reactivity of p-hydroxybenzoate hydroxylase containing 1-deaza-FAD.
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1. Active-site structural comparison of streptococcal NADH peroxidase and NADH oxidase. Reconstitution with artificial flavins.;Journal of Biological Chemistry;1992-02
2. A monoclonal antibody recognizing the FAD-binding site of 4-aminobenzoate hydroxylase from Agaricus bisporus.;Journal of Biological Chemistry;1990-09
3. [24] Hydroxybenzoate hydroxylase;Hydrocarbons and Methylotrophy;1990
4. The temperature and pH dependence of some properties of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens;European Journal of Biochemistry;1989-02
5. Reduction of Substituted Flavins by ·CO−2and Cyclic Disulphide Anions;International Journal of Radiation Biology and Related Studies in Physics, Chemistry and Medicine;1987-01
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