@article{Reichenbecher1996molec-7679,
  year={1996},
  doi={10.1111/j.1432-1033.1996.0406k.x},
  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/RAGE and mass spectrometry},
  number={2},
  volume={237},
  issn={0014-2956},
  journal={European Journal of Biochemistry},
  pages={406--413},
  author={Reichenbecher, Wolfram and Rüdiger, Angelika and Kroneck, Peter M. H. and Schink, Bernhard}
}

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    <dc:creator>Schink, Bernhard</dc:creator>
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    <dc:creator>Reichenbecher, Wolfram</dc:creator>
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    <dcterms:bibliographicCitation>First publ. in: European Journal of Biochemistry 237 (1996), pp. 406-413</dcterms:bibliographicCitation>
    <dc:creator>Rüdiger, Angelika</dc:creator>
    <dcterms:issued>1996</dcterms:issued>
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    <dcterms:abstract xml:lang="eng">The molybdenum-containing iron-sulfur protein 1,2,3,5-tetrahydroxybenzene:1,2,3-trihydroxyben-zene 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 α subunit (100.4 kDa) and a β 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 α and β 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 cofactor. 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 20K); and the Mo(V) center consisting of a multiple signal around g 1.98 (detectable &gt;70 K).</dcterms:abstract>
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    <dc:contributor>Kroneck, Peter M. H.</dc:contributor>
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    <dcterms: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/RAGE and mass spectrometry</dcterms:title>
    <dc:contributor>Schink, Bernhard</dc:contributor>
    <dc:contributor>Rüdiger, Angelika</dc:contributor>
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