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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1990-9-7
|
| pubmed:abstractText |
The interactions of the essential divalent cation, Zn2+, with the binary complex formed between glycerol dehydrogenase (glycerol:NAD+ 2-oxidoreductase, EC 1.1.1.6) and its coenzyme NADH have been examined by fluorescence spectroscopy. Both the metallo and non-metallo form of the enzyme bind the coenzyme NADH. The addition of Zn2+ ions to a solution of the binary complex formed between metal-depleted enzyme and NADH results in a rapid increase in fluorescence emission at 430 nm. This has been used to determine the on rate for Zn2+ to the enzyme/binary complex. A dissociation constant of 3.02 +/- 0.25.10(-9) M for the equilibrium between Zn2+ ions and the enzyme has been determined.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0006-3002
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
1
|
| pubmed:volume |
1040
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
130-3
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:2378897-Geobacillus stearothermophilus,
pubmed-meshheading:2378897-Kinetics,
pubmed-meshheading:2378897-NAD,
pubmed-meshheading:2378897-Oxidation-Reduction,
pubmed-meshheading:2378897-Protein Binding,
pubmed-meshheading:2378897-Spectrometry, Fluorescence,
pubmed-meshheading:2378897-Sugar Alcohol Dehydrogenases,
pubmed-meshheading:2378897-Zinc
|
| pubmed:year |
1990
|
| pubmed:articleTitle |
Studies on the interactions of glycerol dehydrogenase from Bacillus stearothermophilus with Zn2+ ions and NADH.
|
| pubmed:affiliation |
Department of Biochemistry, University of Southampton, U.K.
|
| pubmed:publicationType |
Journal Article
|