Functional Synthetic Model for the Lanthanide-Dependent Quinoid Alcohol Dehydrogenase Active Site.

The oxidation of methanol by dehydrogen-ase enzymes is an essential part of the bacterial methane metabolism cycle. The recent discovery of a lanthanide (Ln) cation in the active site of the XoxF dehydrogenase represents the only example of a rare-earth element in a physiological role. Herein, we re...

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Publicado en:Journal of the American Chemical Society Vol. 140; no. 4; pp. 1223 - 1227
Autores principales: McSkimming, Alex, Cheisson, Thibault, Carroll, Patrick J., Schelter, Eric J.
Formato: Artículo
Publicado: American Chemical Society 1/31/2018
Materias:
Acceso en línea:Ver este registro en EBSCOhost
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        atl: Functional Synthetic Model for the Lanthanide-Dependent Quinoid Alcohol Dehydrogenase Active Site.
      aug:
        au:
          McSkimming, Alex
          Cheisson, Thibault
          Carroll, Patrick J.
          Schelter, Eric J.
        affil: P. Roy and Diana T. Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, 231 S 34th Street, Philadelphia, Pennsylvania 19104, United States
      su:
        Quinoidine
        Catalytic dehydrogenation
        Density functional theory
        Alcohol dehydrogenase
        Oxidation of methanol
      sug:
        subj:
          Quinoidine
          Catalytic dehydrogenation
          Density functional theory
          Alcohol dehydrogenase
          Oxidation of methanol
      ab: The oxidation of methanol by dehydrogen-ase enzymes is an essential part of the bacterial methane metabolism cycle. The recent discovery of a lanthanide (Ln) cation in the active site of the XoxF dehydrogenase represents the only example of a rare-earth element in a physiological role. Herein, we report the first synthetic, functional model of Ln-dependent dehydrogenase and its stoichiometric and catalytic dehydrogenation of a benzyl alcohol. Density functional theory calculations implicate a hydride transfer mechanism for these reactions.
      pubtype: Academic Journal
      doctype: Article
      src: R
    language: English
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