Studies on the interactions of glycerol dehydrogenase from Bacillus stearothermophilus with Zn2+ ions and NADH.
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.
Spencer
P
P
Department of Biochemistry, University of Southampton, U.K.
Slade
A
A
Atkinson
T
T
Gore
M G
MG
D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D007700:Kinetics; D009243:NAD / Q000494:pharmacology*; D010084:Oxidation-Reduction; D011485:Protein Binding; D013050:Spectrometry, Fluorescence; D013401:Sugar Alcohol Dehydrogenases / Q000378:metabolism*; D015032:Zinc / Q000494:pharmacology*
D009243:NAD; D013401:Sugar Alcohol Dehydrogenases; C020672:glycerol dehydrogenase; D015032:Zinc