1459949

Source:http://linkedlifedata.com/resource/pubmed/id/1459949

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0211333, umls-concept:C1265186, umls-concept:C1880022, umls-concept:C1998793
pubmed:issue	24
pubmed:dateCreated	1993-1-11
pubmed:abstractText	Tetrachloro-p-hydroquinone (TeCH) is the first intermediate in pentachlorophenol (PCP) degradation by Flavobacterium sp. strain ATCC 39723. We previously purified a PCP hydroxylase that oxidized PCP to TeCH. Subsequently, we identified the reductive dehalogenation of TeCH to 2,3,6-trichloro-p-hydroquinone and then to 2,6-dichloro-p-hydroquinone in a cell extract with the reduced form of glutathione as the reducing agent under anaerobic conditions. Here we report the purification of a TeCH reductive dehalogenase that reductively dehalogenated TeCH to trichlorohydroquinone and then to dichlorohydroquinone. The enzyme was purified by protamine sulfate treatment, ammonium sulfate fractionation, and phenyl-agarose, anion-exchange, and gel filtration column chromatographies. As determined by gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis analyses, the protein has a molecular weight of about 30,000; nondenaturing polyacrylamide gel electrophoresis analysis suggests that the native enzyme exists as a dimer. The enzyme used glutathione but not NADPH, NADH, dithiothreitol, or ascorbic acid as the reducing agent. The optimal pH was close to neutral.
pubmed:commentsCorrections	http://linkedlifedata.com/resource/pubmed/commentcorrection/1459949-1569020, http://linkedlifedata.com/resource/pubmed/commentcorrection/1459949-1731793, http://linkedlifedata.com/resource/pubmed/commentcorrection/1459949-2066340, http://linkedlifedata.com/resource/pubmed/commentcorrection/1459949-2104602, http://linkedlifedata.com/resource/pubmed/commentcorrection/1459949-3059995, http://linkedlifedata.com/resource/pubmed/commentcorrection/1459949-3145740, http://linkedlifedata.com/resource/pubmed/commentcorrection/1459949-3801030, http://linkedlifedata.com/resource/pubmed/commentcorrection/1459949-4091568, http://linkedlifedata.com/resource/pubmed/commentcorrection/1459949-500718, http://linkedlifedata.com/resource/pubmed/commentcorrection/1459949-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/1459949-7304929
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/2985120R
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/2,3,5,6-tetrachlorohydroquinone, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Hydroquinones
pubmed:status	MEDLINE
pubmed:month	Dec
pubmed:issn	0021-9193
pubmed:author	pubmed-author:OrserC SCS, pubmed-author:TUY CYC, pubmed-author:ToppEE
pubmed:issnType	Print
pubmed:volume	174
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	8003-7
pubmed:dateRevised	2010-9-7
pubmed:meshHeading	pubmed-meshheading:1459949-Amino Acid Sequence, pubmed-meshheading:1459949-Bacterial Proteins, pubmed-meshheading:1459949-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:1459949-Flavobacterium, pubmed-meshheading:1459949-Hydrolases, pubmed-meshheading:1459949-Hydroquinones, pubmed-meshheading:1459949-Molecular Sequence Data
pubmed:year	1992
pubmed:articleTitle	Purification and characterization of a tetrachloro-p-hydroquinone reductive dehalogenase from a Flavobacterium sp.
pubmed:affiliation	Department of Bacteriology and Biochemistry, University of Idaho, Moscow 83843.
pubmed:publicationType	Journal Article, Research Support, U.S. Gov't, Non-P.H.S.