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pubmed-article:2378897pubmed:abstractTextThe 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.lld:pubmed
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pubmed-article:2378897pubmed:dateRevised2009-11-19lld:pubmed
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pubmed-article:2378897pubmed:year1990lld:pubmed
pubmed-article:2378897pubmed:articleTitleStudies on the interactions of glycerol dehydrogenase from Bacillus stearothermophilus with Zn2+ ions and NADH.lld:pubmed
pubmed-article:2378897pubmed:affiliationDepartment of Biochemistry, University of Southampton, U.K.lld:pubmed
pubmed-article:2378897pubmed:publicationTypeJournal Articlelld:pubmed