| pubmed-article:16346490 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16346490 | lifeskim:mentions | umls-concept:C0038661 | lld:lifeskim |
| pubmed-article:16346490 | lifeskim:mentions | umls-concept:C0085470 | lld:lifeskim |
| pubmed-article:16346490 | lifeskim:mentions | umls-concept:C0054860 | lld:lifeskim |
| pubmed-article:16346490 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:16346490 | pubmed:dateCreated | 2010-6-25 | lld:pubmed |
| pubmed-article:16346490 | pubmed:abstractText | 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 x 10 sec for 3-chlorocatechol and 2.38 x 10 sec for 3-fluorocatechol. The inhibitor constants (K(i)) were 23 muM for 3-chlorocatechol and 17 muM 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. | lld:pubmed |
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| pubmed-article:16346490 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16346490 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16346490 | pubmed:status | PubMed-not-MEDLINE | lld:pubmed |
| pubmed-article:16346490 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:16346490 | pubmed:issn | 0099-2240 | lld:pubmed |
| pubmed-article:16346490 | pubmed:author | pubmed-author:KnackmussH... | lld:pubmed |
| pubmed-article:16346490 | pubmed:author | pubmed-author:ReinekeWW | lld:pubmed |
| pubmed-article:16346490 | pubmed:author | pubmed-author:BartelsII | lld:pubmed |
| pubmed-article:16346490 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16346490 | pubmed:volume | 47 | lld:pubmed |
| pubmed-article:16346490 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16346490 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16346490 | pubmed:pagination | 500-5 | lld:pubmed |
| pubmed-article:16346490 | pubmed:dateRevised | 2010-9-20 | lld:pubmed |
| pubmed-article:16346490 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:16346490 | pubmed:articleTitle | Suicide Inactivation of Catechol 2,3-Dioxygenase from Pseudomonas putida mt-2 by 3-Halocatechols. | lld:pubmed |
| pubmed-article:16346490 | pubmed:affiliation | Gesellschaft für Strahlen- und Umweltforschung mbH, Munich, and Lehrstuhl für Chemische Mikrobiologie der Universität-Gesamthochschule, D-5600 Wuppertal 1, Federal Republic of Germany. | lld:pubmed |
| pubmed-article:16346490 | pubmed:publicationType | Journal Article | lld:pubmed |
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