Abstract
Medium-chain dehydrogenases/reductases of the liver alcohol dehydrogenase type are zinc metalloenzymes (Vallee and Hoch, 1957; IAeson, 1964; Drum et al., 1969), with two zinc atoms per subunit, one catalytic at the active site and one structural at a site influencing subunit interactions (Sytkowski and Vallee, 1976; Branden et al., 1975). In horse liver alcohol dehydrogenase and in all other mammalian liver forms, the structural zinc atom is liganded by four closely spaced Cys residues, at positions 97, 100, 103, and III (Branden et al., 1975; Vallee and Auld, 1990). The mechanism by which this zinc atom maintains its structural role is largely unknown. To probe the metal-binding characteristics of the structural zinc site of alcohol dehydrogenase, we have analyzed zinc-binding to a synthetic replica of the protein segment containing the four Cys residues and covering residues 93–115 of the parent molecule.
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