| pubmed-article:2066340 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2066340 | lifeskim:mentions | umls-concept:C1265186 | lld:lifeskim |
| pubmed-article:2066340 | lifeskim:mentions | umls-concept:C0080194 | lld:lifeskim |
| pubmed-article:2066340 | lifeskim:mentions | umls-concept:C0016223 | lld:lifeskim |
| pubmed-article:2066340 | lifeskim:mentions | umls-concept:C0598079 | lld:lifeskim |
| pubmed-article:2066340 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:2066340 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:2066340 | lifeskim:mentions | umls-concept:C0135909 | lld:lifeskim |
| pubmed-article:2066340 | pubmed:issue | 14 | lld:pubmed |
| pubmed-article:2066340 | pubmed:dateCreated | 1991-8-14 | lld:pubmed |
| pubmed-article:2066340 | pubmed:abstractText | A pentachlorophenol (PCP) hydroxylase which catalyzed the conversion of PCP to 2,3,5,6-tetrachlorohydroquinone and released iodide from triiodophenol in the presence of NADPH and oxygen was identified. The enzyme was purified by protamine sulfate precipitation, ammonium sulfate precipitation, hydrophobic chromatography, anion-exchange chromatography, gel filtration chromatography, and crystallization. The enzyme was a monomer with a molecular weight of 63,000. Under certain conditions, dimer and multimer conformations were also observed. The pI of the enzyme was pH 4.3. The optimal conditions for activity were a pH of 7.5 to 8.5 and a temperature of 40 degrees C. Each enzyme molecule contained one flavin adenine dinucleotide molecule. The Km for PCP was 30 microM and the Vmax was 16 mumol/min/mg of protein. The enzymatic reaction required 2 mol of NADPH per mol of halogenated substrate. On the basis of the data we present, it is likely that PCP hydroxylase is a flavoprotein monooxygenase. The addition of flavins to the reaction mixture did not stimulate the enzymatic reaction; however, we identified the photodegradation of triiodophenol and tribromophenol, but not PCP, by flavin mononucleotide or riboflavin and light. | lld:pubmed |
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| pubmed-article:2066340 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2066340 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2066340 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2066340 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2066340 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2066340 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:2066340 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:2066340 | pubmed:author | pubmed-author:TUY CYC | lld:pubmed |
| pubmed-article:2066340 | pubmed:author | pubmed-author:OrserC SCS | lld:pubmed |
| pubmed-article:2066340 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2066340 | pubmed:volume | 173 | lld:pubmed |
| pubmed-article:2066340 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2066340 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2066340 | pubmed:pagination | 4447-53 | lld:pubmed |
| pubmed-article:2066340 | pubmed:dateRevised | 2010-9-9 | lld:pubmed |
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| pubmed-article:2066340 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:2066340 | pubmed:articleTitle | Purification and properties of pentachlorophenol hydroxylase, a flavoprotein from Flavobacterium sp. strain ATCC 39723. | lld:pubmed |
| pubmed-article:2066340 | pubmed:affiliation | Department of Bacteriology and Biochemistry, University of Idaho, Moscow 83843. | lld:pubmed |
| pubmed-article:2066340 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2066340 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:2066340 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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