Literature Seminar Abstract:

Metalloenzymes drive chemical processes across life forms and mimicking this reactivity still remains a synthetic challenge. Almost all metalloenzyme active sites are composed of transition metals. In 2007 in volcanic mudpools in southern Italy, the bacteria Methylacidiphilum fumariolicum was discovered with an enzyme containing a lanthanide active site in a methanol dehydrogenase enzyme. This is the first report of a lanthanide ion acting in a biological role. To add insight into this reactivity, a recent report by McSkimming et. al. describes the first synthetic model of this enzyme’s active site and its stoichiometric and catalytic dehydrogenation of a benzyl alcohol. Furthermore, density functional theory calculations indicate a hydride transfer mechanism is favored as the mechanistic pathway of dehydrogenation. In their report, they showed the first lanthanide quinoline quinone complex acting as a dehydrogenation catalyst under neutral and basic conditions.