The inhibition of malate dehydrogenase by chlorammine-platinum complexes.
Abstract Equilibrium association constants have been calculated for various platinum (II) and platinum (IV) complexes. The association constants were greatest for the dinegatively charged state, regardless of the valence state of the platinum, and the constant decreased considerably as the charge increased. There were no measurable values for positively charged complex states. The conclusion is that the electrostatic charge of the platinum complex is the most important factor causing the inhibition of the enzyme, and the steric differences have only a minor effect, while geometric variation as in the comparison of cis and trans dichlorodiamine-platinum (II) isomers yields no differences in inhibition.