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Structural, spectroscopic and catalytic activity studies on glutathione reductase reconstituted with FAD analogues

Structural, spectroscopic and catalytic activity studies on glutathione reductase reconstituted with FAD analogues

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ERMLER, Ulrich, Sandro GHISLA, Vincent MASSEY, Georg E. SCHULZ, 1991. Structural, spectroscopic and catalytic activity studies on glutathione reductase reconstituted with FAD analogues. In: European Journal of Biochemistry. 199(1), pp. 133-138. ISSN 0014-2956. eISSN 1432-1033

@article{Ermler1991Struc-7614, title={Structural, spectroscopic and catalytic activity studies on glutathione reductase reconstituted with FAD analogues}, year={1991}, doi={10.1111/j.1432-1033.1991.tb16100.x}, number={1}, volume={199}, issn={0014-2956}, journal={European Journal of Biochemistry}, pages={133--138}, author={Ermler, Ulrich and Ghisla, Sandro and Massey, Vincent and Schulz, Georg E.} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/7614"> <dcterms:abstract xml:lang="eng">FAD-modified human glutathione reductases were reconstituted from apoenzyme using the FAD analogues 6-SH-FAD, 6-SCN-FAD, 6-OH-FAD, 6-NH2-FAD and 8-OH-FAD. The catalytic activities of the modified enzymes were substantially lower than for the native enzyme. All five species could be crystallized, but only those containing 6-SH-FAD, 6-OH-FAD and 6-NH2-FAD yielded crystals that could be analyzed. X-ray analyses and structural refinements were performed at 0.27 nm and 0.30 nm resolution resulting in R factors around 13.5%. The crystal structures showed the additional non-hydrogen atoms and small conformational changes of the polypeptide that were obviously induced by the substituents of the FAD analogues. The observed changes together with spectroscopic and activity data permit some conclusions about the chemical nature of the substituents.</dcterms:abstract> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dc:contributor>Massey, Vincent</dc:contributor> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:35:48Z</dc:date> <dc:contributor>Ermler, Ulrich</dc:contributor> <dc:creator>Ermler, Ulrich</dc:creator> <dc:contributor>Schulz, Georg E.</dc:contributor> <dc:language>eng</dc:language> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/7614"/> <dc:creator>Schulz, Georg E.</dc:creator> <dc:creator>Massey, Vincent</dc:creator> <dc:format>application/pdf</dc:format> <dc:rights>deposit-license</dc:rights> <dc:contributor>Ghisla, Sandro</dc:contributor> <dc:creator>Ghisla, Sandro</dc:creator> <dcterms:issued>1991</dcterms:issued> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:35:48Z</dcterms:available> <dcterms:title>Structural, spectroscopic and catalytic activity studies on glutathione reductase reconstituted with FAD analogues</dcterms:title> <dcterms:bibliographicCitation>First publ. in: European Journal of Biochemistry 199 (1991), 1, pp. 133-138</dcterms:bibliographicCitation> </rdf:Description> </rdf:RDF>

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