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	Author	Andersson, P.; Kvassman, J.; Lindstrom, A.; Olden, B.; Pettersson, G.
	Title	Effect of NADH on the pKa of zinc-bound water in liver alcohol dehydrogenase			Type	Journal Article
	Year	1981	Publication	European Journal of Biochemistry / FEBS	Abbreviated Journal	Eur J Biochem
	Volume	113	Issue	3	Pages	425-433
	Keywords	Alcohol Oxidoreductases/metabolism; Aldehydes/metabolism; Animals; Binding Sites; Cinnamates/metabolism; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Liver/metabolism; NAD/*metabolism; Water/metabolism; Zinc/metabolism
	Abstract	Equilibrium constants for coenzyme binding to liver alcohol dehydrogenase have been determined over the pH range 10--12 by pH-jump stop-flow techniques. The binding of NADH or NAD+ requires the protonated form of an ionizing group (distinct from zinc-bound water) with a pKa of 10.4. Complex formation with NADH exhibits an additional dependence on the protonation state of an ionizing group with a pKa of 11.2. The binding of trans-N,N-dimethylaminocinnamaldehyde to the enzyme . NADH complex is prevented by ionization of the latter group. It is concluded from these results that the pKa-11.2-dependence of NADH binding most likely derives from ionization of the water molecule bound at the catalytic zinc ion of the enzyme subunit. The pKa value of 11.2 thus assigned to zinc-bound water in the enzyme . NADH complex appears to be typical for an aquo ligand in the inner-sphere ligand field provided by the zinc-binding amino acid residues in liver alcohol dehydrogenase. This means that the pKa of metal-bound water in zinc-containing enzymes can be assumed to correlate primarily with the number of negatively charged protein ligands coordinated by the active-site zinc ion.
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	Corporate Author				Thesis
	Publisher		Place of Publication		Editor
	Language	English	Summary Language		Original Title
	Series Editor		Series Title		Abbreviated Series Title
	Series Volume		Series Issue		Edition
	ISSN	0014-2956	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:7011796			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3810
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