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http://purl.uniprot.org/citations/8647079http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8647079http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8647079http://www.w3.org/2000/01/rdf-schema#comment"The molybdenum-containing iron-sulfur protein 1,2,3,5-tetrahydroxybenzene: 1,2,3-trihydroxybenzene hydroxyltransferase (transhydroxylase) of Pelobacter acidigallici was investigated by various techniques including mass spectrometry and electron paramagnetic resonance. Mass spectrometry confirmed that the 133-kDa protein is a heterodimer consisting of an alpha subunit (100.4 kDa) and a beta subunit (31.3 kDa). The presence of a molybdenum cofactor was documented by fluorimetric analysis of the oxidized form A of molybdopterin. The enzyme contained 1.55 +/- 0.14 mol pterin and 0.92 +/-0.25 mol molybdenum/mol enzyme (133 kDa). Alkylation of the molybdenum cofactor with iodoacetamide formed di(carboxamidomethyl)-molybdopterin. Upon acid hydrolysis, 1.4 mol 5'GMP/mol enzyme (133 kDa) was released indicating that molybdenum is bound by a molybdopterin guanine dinucleotide. The alpha and beta subunits were separated by preparative gel electrophoresis. Both subunit fractions were free of molybdenum but contained equal amounts of a fluorescent form of the molybdenum cofactors. Mass spectrometry at various pH values revealed that an acid-labile cofactor was released from the large subunit and also from the small subunit. At X-band, 5-25 K, transhydroxylase (as isolated) showed minor EPR resonances with apparent g values around 4.3, 2.03 and, depending on the preparation, a further signal at g of approximately 1.98. This signal was still detectable above 70 K and was attributed to a Mo(V) center. Upon addition of dithionite, a complex set of intense resonances appeared in the region g 2.08-1.88. From their temperature dependence, three distinct sites could be identified: the Fe-S center I with gx,y,z at approximately 1.875, 1.942 and 2.087 (gav 1.968, detectable < 20 K); the Fe-S center II with gx,y,z at approximately 1.872, 1.955 and 2.051 (gav 1.959, detectable > 20 K); and the Mo(V) center consisting of a multiple signal around g 1.98 (detectable > 70 K)."xsd:string
http://purl.uniprot.org/citations/8647079http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1996.0406k.x"xsd:string
http://purl.uniprot.org/citations/8647079http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1996.0406k.x"xsd:string
http://purl.uniprot.org/citations/8647079http://purl.uniprot.org/core/author"Kroneck P.M.H."xsd:string
http://purl.uniprot.org/citations/8647079http://purl.uniprot.org/core/author"Kroneck P.M.H."xsd:string
http://purl.uniprot.org/citations/8647079http://purl.uniprot.org/core/author"Schink B."xsd:string
http://purl.uniprot.org/citations/8647079http://purl.uniprot.org/core/author"Schink B."xsd:string
http://purl.uniprot.org/citations/8647079http://purl.uniprot.org/core/author"Reichenbecher W."xsd:string
http://purl.uniprot.org/citations/8647079http://purl.uniprot.org/core/author"Reichenbecher W."xsd:string
http://purl.uniprot.org/citations/8647079http://purl.uniprot.org/core/author"Ruediger A."xsd:string
http://purl.uniprot.org/citations/8647079http://purl.uniprot.org/core/author"Ruediger A."xsd:string
http://purl.uniprot.org/citations/8647079http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8647079http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8647079http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/8647079http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/8647079http://purl.uniprot.org/core/pages"406-413"xsd:string
http://purl.uniprot.org/citations/8647079http://purl.uniprot.org/core/pages"406-413"xsd:string
http://purl.uniprot.org/citations/8647079http://purl.uniprot.org/core/title"One molecule of molybdopterin guanine dinucleotide is associated with each subunit of the heterodimeric Mo-Fe-S protein transhydroxylase of Pelobacter acidigallici as determined by SDS/PAGE and mass spectrometry."xsd:string
http://purl.uniprot.org/citations/8647079http://purl.uniprot.org/core/title"One molecule of molybdopterin guanine dinucleotide is associated with each subunit of the heterodimeric Mo-Fe-S protein transhydroxylase of Pelobacter acidigallici as determined by SDS/PAGE and mass spectrometry."xsd:string
http://purl.uniprot.org/citations/8647079http://purl.uniprot.org/core/volume"237"xsd:string
http://purl.uniprot.org/citations/8647079http://purl.uniprot.org/core/volume"237"xsd:string
http://purl.uniprot.org/citations/8647079http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8647079
http://purl.uniprot.org/citations/8647079http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8647079
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