Extradiol Cleavage of 3-Methylcatechol by Catechol 1,2-Dioxygenase from Various Microorganisms
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چکیده
منابع مشابه
Extradiol cleavage of 3-methylcatechol by catechol 1,2-dioxygenase from various microorganisms.
The isofunctional enzymes of catechol 1,2-dioxygenase from species of Acinetobacter, Pseudomonas, Nocardia, Alcaligenes, and Corynebacterium oxidize 3-methylcatechol according to both the intradiol and extradiol cleavage patterns. However, the enzyme preparations from Brevibacterium and Arthrobacter have only the intradiol cleavage activity. Comparison of substrate specificity among these isofu...
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A 2,3-dihydroxybiphenyl 1,2-dioxygenase from the naphthalenesulfonate-degrading bacterium Sphingomonas sp. strain BN6 oxidized 3-chlorocatechol to a yellow product with a strongly pH-dependent absorption maximum at 378 nm. A titration curve suggested (de)protonation of an ionizable group with a pKa of 4.4. The product was isolated, purified, and converted, by treatment with diazomethane, to a d...
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An iron(III)-catecholate complex of a facial tridentate ligand reacts with dioxygen in the presence of ammonium acetate-acetic acid buffer to cleave the aromatic C-C bond of 3,5-di-tert-butylcatechol regiospecifically resulting in the formation of an extradiol product with multiple turnovers.
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ژورنال
عنوان ژورنال: Applied and Environmental Microbiology
سال: 1977
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.33.3.725-727.1977