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Mössbauer characterization of the Fe−S center in the catalytic metal binding site of alcohol dehydrogenase

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Abstract

Iron in its divalent and trivalent form can be substituted in the catalytic zinc site of alcohol dehydrogenase from horse liver (HLADH). Fe-HLADH in either oxidation state does not show enzymatic activity in the oxidation of ethanol. Nevertheless, Mössbauer studies of this material are of considerable interest, because they elucidate the effect of pH and coenzyme-induced conformational changes of the protein on the metal ion. It is of importance to note that zinc itself due to the lack of suitable chromophoric and magnetic properties does not provide any comparable information.

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Authors and Affiliations

  1. Analytische und Biologische Chemie, Univ. des Saarlandes, 6600, Saarbrücken, FRG

    C. Haas, W. Maret & M. Zeppezauer

  2. Institut für Weinchemie und Getränketechnologie, Forschungsanstalt Geisenheim, 6222, Geisenheim, FRG

    H. Dietrich

  3. Institut für Physik, Medizinische Universität zu Lübeck, 2400, Lübeck, FRG

    R. Montiel-Montoya, E. Bill & A. X. Trautwein

Authors
  1. C. Haas
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  2. H. Dietrich
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  3. W. Maret
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  4. M. Zeppezauer
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  5. R. Montiel-Montoya
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  6. E. Bill
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  7. A. X. Trautwein
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Haas, C., Dietrich, H., Maret, W. et al. Mössbauer characterization of the Fe−S center in the catalytic metal binding site of alcohol dehydrogenase. Hyperfine Interact 29, 1419–1422 (1986). https://doi.org/10.1007/BF02399500

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  • DOI: https://doi.org/10.1007/BF02399500

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