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1 kwi 2010 · Different zinc complexes postulated during the LADH-catalyzed dehydrogenation of alcohol: (a) “Classical” mechanism (e.g. [63]); (b) molecule of water takes part in the reaction [53]; (c) Glu-67 or Glu-68 can be intermittently bonded to the zinc [57], [58].
The coordination chemistry of the zinc ion in the active site of alcohol dehydrogenase has been studied by the ab initio Hartree-Fock method. Geometry optimisations were performed using analytical gradients and basis sets of double zeta quality. Correlation effects were included at the MP2 level.
1 gru 2002 · This review is a summary of our current knowledge of the structure, function and mechanism of action of the three zinc-containing alcohol dehydrogenases, YADH-1, YADH-2 and YADH-3, in baker’s yeast, Saccharomyces cerevisiae.
The role of zinc in the catalytic action of yeast alcohol dehydro- genase has been studied through the kinetics of the inhibition of activity by chelating agents (I), particularly...
zinc ion appears to be tetrahedrally coordinated with one water molecule (or hydroxide ion, depending on pH) as the fourth first-sphere ligand. The most widely accepted reaction mechanism for alcohol dehydrogenase [1] consists of (Scheme 1): (1) binding of NAD+; (2) binding of the alcohol substrate by
Zinc-containing ADHs frequently have two tetrahedrally coordinated zinc ions per subunit, one catalytic at the active site and one non-catalytic at a site influencing structural integrity and subunit interactions. This entry summarizes general properties of ADH structural zinc sites.
1 maj 2000 · These studies demonstrate that the chemical nature of the direct ligands and the structure of the surrounding hydrogen bond network are crucial for both the activity of carbonic anhydrase and the metal ion affinity of the zinc-binding site.
