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Inhibition of horse-liver alcohol dehydrogenase by Pt(CN)4 2- and Au(CN)2-.

Single and multiple-inhibition experiments provide evidence that the complex anion Pt(CN)42- is bound at a single site per subunit of liver alcohol dehydrogenase in strict competition with coenzyme, ADP-ribose, AMP and (less than 100 mM) chloride ion, but independently of 1,10-phenanthroline. Binding of adenosine decreases the stability constant for the enzyme · Pt(CN)42- complex from 16 mM-1 to 4 mM-1. 
 
 
 
Au(CN)2- is bound at two sites per subunit of the enzyme. Both interactions are competitive with coenzyme, ADP-ribose and AMP, but independent of 1,10-phenanthroline. Only one site is available for interaction with Au(CN)2- in the binary enzyme complexes formed with Pt(CN)42-, chloride ion, or adenosine. Estimation of the corresponding binding constants for Au(CN)2- gave evidence for cooperativity between the two Au(CN)2- binding sites. 
 
 
 
These results strongly indicate that Pt(CN)42- is bound at a site within the protein region occupied by the phosphate groups of the coenzyme, and it is suggested that arginine-47 in the enzymatic amino-acid sequence is part of a common binding site for negative charges on the coenzyme and coenzyme competitive anions such as Pt(CN)42-, Au(CN)2-, chloride and iodoacetate. The second binding site for Au(CN)2- appears to be situated within the protein region occupied by the adenosine part of the coenzyme.