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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1975-6-27
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pubmed:abstractText |
The binding of Au(CN)2- and Pt(CN)4-2- ions to the coenzyme binding site of horse liver alcohol dehydrogenase (alcohol : NAD+ oxidoreductase EC 1.1.1.1) has been studied by 35C1 nuclear magnetic relaxation. Longitudinal relaxation rates were analyzed in terms of a simple model and binding constants for Au(CN)2-, Pt(CN)4-2- and C1- were estimated. From a comparison between transverse and longitudinal relaxation rates the correlation time and the quadrupole coupling constant of bound chloride ion were obtained. The quadrupole coupling constant estimated from a simple electrostatic model for chloride ion interacting with an arginine group agrees with the experimental value.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0006-3002
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
377
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:164218-Alcohol Oxidoreductases,
pubmed-meshheading:164218-Animals,
pubmed-meshheading:164218-Arginine,
pubmed-meshheading:164218-Binding Sites,
pubmed-meshheading:164218-Chlorine,
pubmed-meshheading:164218-Cyanides,
pubmed-meshheading:164218-Gold,
pubmed-meshheading:164218-Horses,
pubmed-meshheading:164218-Liver,
pubmed-meshheading:164218-Magnetic Resonance Spectroscopy,
pubmed-meshheading:164218-Models, Chemical,
pubmed-meshheading:164218-NAD,
pubmed-meshheading:164218-Platinum,
pubmed-meshheading:164218-Protein Binding,
pubmed-meshheading:164218-Radioisotopes
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pubmed:year |
1975
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pubmed:articleTitle |
Binding of Au(CN)2- and Pt(CN)4-2- to horse liver alcohol dehydrogenase. A 35C1NMR relaxation study.
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pubmed:publicationType |
Journal Article
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