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- W1555471713 abstract "The inactivation of catechol 2,3-dioxygenase from Pseudomonas putida mt-2 by 3-chloro- and 3-fluorocatechol and the iron-chelating agent Tiron (catechol-3,5-disulfonate) was studied. Whereas inactivation by Tiron is an oxygen-independent and mostly reversible process, inactivation by the 3-halocatechols was only observed in the presence of oxygen and was largely irreversible. The rate constants for inactivation ( K 2 ) were 1.62 × 10 −3 sec −1 for 3-chlorocatechol and 2.38 × 10 −3 sec −1 for 3-fluorocatechol. The inhibitor constants ( K i ) were 23 μM for 3-chlorocatechol and 17 μM for 3-fluorocatechol. The kinetic data for 3-fluorocatechol could only be obtained in the presence of 2-mercaptoethanol. Besides inactivated enzyme, some 2-hydroxyhexa-2,4-diendioic acid was formed from 3-chlorocatechol, suggesting 5-chloroformyl-2-hydroxypenta-2,4-dienoic acid as the actual suicide product of meta -cleavage. A side product of 3-fluorocatechol cleavage is a yellow compound with the spectral characteristics of a 2-hydroxy-6-oxohexa-2,4-dienoic acid indicating 1,6-cleavage. Rates of inactivation by 3-fluorocatechol were reduced in the presence of superoxide dismutase, catalase, formate, and mannitol, which implies that superoxide anion, hydrogen peroxide, and hydroxyl radical exhibit additional inactivation." @default.
- W1555471713 created "2016-06-24" @default.
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- W1555471713 date "1984-03-01" @default.
- W1555471713 modified "2023-10-18" @default.
- W1555471713 title "Suicide Inactivation of Catechol 2,3-Dioxygenase from <i>Pseudomonas putida</i> mt-2 by 3-Halocatechols" @default.
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- W1555471713 doi "https://doi.org/10.1128/aem.47.3.500-505.1984" @default.
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