Hydroxylation of o-halogenophenol and o-nitrophenol by salicylate hydroxylase.

Hydroxylation of o-halogenophenol and o-nitrophenol by salicylate hydroxylase. Research Abstract Details 

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Hydroxylation of o-halogenophenol and o-nitrophenol by salicylate hydroxylase. Abstract Text:

K Suzuki,T Gomi,T Kaidoh,E Itagaki,

Salicylate hydroxylase [EC 1.14.13.1] from Pseudomonas putida catalyzed the formation of catechol from substrate analogues such as o-nitro-, o-amino-, o-iodo-, o-bromo-, and o-chloro-phenol by removing the ortho-substituted groups. They are converted into nitrite, ammonia, and halide ions, respectively. Kinetic parameters of these reactions were determined by spectrophotometric and polarographic methods. Hydroxylation of o-nitro- or o-iodophenol proceeds with the unusual stoichiometry of 2:1:1 for consumed NADH, O2-uptake, and catechol formed. Other ortho-substituted phenols examined also gave the same results. Like salicylate, these substrates perturb the absorption spectrum of salicylate hydroxylase in the visible region, indicating the formation of enzyme.substrate complexes. Titration experiments with ortho-substituted phenols gave the dissociation constants of the complexes. The complexes were quantitatively reduced with NADH or dithionite without detectable formation of the intermediates. The fact that one atom of 18O2 was incorporated into the produced catechol in hydroxylation of o-nitrophenol indicates that the reaction is of monooxygenase nature. It is concluded that salicylate hydroxylase cleaves the C-N and C-X bonds of ortho-substituted phenols.

Hydroxylation of o-halogenophenol and o-nitrophenol by salicylate hydroxylase. Publishing Authors By Initials

K Suzuki,T Gomi,T Kaidoh,E Itagaki,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research

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Hydroxylation of o-halogenophenol and o-nitrophenol by salicylate hydroxylase. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 109

Page Numbers: 348-53

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Feb

YEAR: 1991

Hydroxylation of o-halogenophenol and o-nitrophenol by salicylate hydroxylase. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Hydroxylation of o-halogenophenol and o-nitrophenol by salicylate hydroxylase. Keywords Mesh Terms:

KEYWORDS: Substrate Specificity

MESH TERMS: enzymology

Chemical & Substance for Abstract: Hydroxylation of o-halogenophenol and o-nitrophenol by salicylate hydroxylase. Information

Substance Name: salicylate 1-monooxygenase

Registry Number: EC 1.14.13.1

Grant and Affiliation Information for Hydroxylation of o-halogenophenol and o-nitrophenol by salicylate hydroxylase.

AFFILIATION: Department of Chemistry, Faculty of Science, Kanazawa University, Ishikawa.

Country: JAPAN

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MEDLINETA: J Biochem

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