Description:
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<jats:list-item><jats:p>Aldehyde binding to liver alcohol dehydrogenase in the absence and presence of coenzymes has been characterized by spectrometric equilibrium methods, using auramine O and bipyridine as reporter ligands.</jats:p></jats:list-item>
<jats:list-item><jats:p>Free enzyme shows a significant affinity for aldehydes, and equilibrium constants for dissociation of the binary complexes formed with typical aldehyde substrates are reported. Binary‐complex formation does not lead to any detectable inner‐sphere coordination of aldehydes to the catalytic zinc ion of the enzyme subunit.</jats:p></jats:list-item>
<jats:list-item><jats:p>Complex formation with NAD<jats:sup>+</jats:sup> or NADH increases the affinity of the enzyme for aromatic aldehydes by a factor of 1.8–3.5 and 6–17, respectively. Benzaldehyde and dimethylaminocinnamaldehyde binding to the enzyme · NAD<jats:sup>+</jats:sup> complex is not detectably associated with inner‐sphere coordination of the aldehyde to zinc.</jats:p></jats:list-item>
<jats:list-item><jats:p>It is concluded that binding of NADH is required to induce catalytically adequate bonding interactions between enzyme and aromatic aldehydes. The effect of reduced coenzyme in this respect is attributed to hydrophobic interactions leading to dehydration of the active‐site region, which allows aldehyde substrates to compete successfully with water for inner‐sphere coordination to the catalytic zinc ion. Oxidized coenzyme is proposed to have a similar promoting effect on metal coordination of aldehydes which function as substrates for the dismutase activity of the enzyme.</jats:p></jats:list-item>
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