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SUMMARY:Discovery and Synthetic Model of Biocatalysis Using Lanthanides
LOCATION:Chemistry A101
TZID:America/Denver
DTSTART:20189101T000000
UID:2026-04-24-02-36-29@natsci.colostate.edu
DTSTAMP:20260424T023629
Description:Literature Seminar Abstract:\n\nMetalloenzymes drive chemical p
 rocesses across life forms and mimicking this reactivity still remains a s
 ynthetic challenge. Almost all metalloenzyme active sites are composed of 
 transition metals. In 2007 in volcanic mudpools in southern Italy\, the ba
 cteria Methylacidiphilum fumariolicum was discovered with an enzyme contai
 ning 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 i
 nsight into this reactivity\, a recent report by McSkimming et. al. descri
 bes the first synthetic model of this enzyme’s active site and its stoic
 hiometric and catalytic dehydrogenation of a benzyl alcohol. Furthermore\,
  density functional theory calculations indicate a hydride transfer mechan
 ism is favored as the mechanistic pathway of dehydrogenation. In their rep
 ort\, they showed the first lanthanide quinoline quinone complex acting as
  a dehydrogenation catalyst under neutral and basic conditions. 4:00 pm
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