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SUMMARY:De novo lanthanide enzymes – from protein dynamics to photoredox
  catalysis +CH636
DTSTART:20240514T161500
DTEND:20240514T171500
DTSTAMP:20260314T212334Z
UID:5cc9f68ff23d9cba1fb4512246502b0c068f4b8bed7c29a9634273f7
CATEGORIES:Conferences - Seminars
DESCRIPTION:Cathleen Zeymer\nAbstract:\nA major challenge in biocatalysis 
 is the development of novel enzymes for reactions beyond nature’s synthe
 tic repertoire. Our approach combines rational design and directed evoluti
 on to generate artificial metalloenzymes and photoenzymes. We recently rep
 orted a de novo protein scaffold with femtomolar affinity for lanthanide i
 ons. These metal cofactors are not only potent Lewis acid catalysts\, some
  of them also promote photoredox chemistry. We have been characterizing th
 e interplay between functional protein dynamics and metal coordination in 
 these systems with various biophysical techniques and developed a cerium-d
 ependent photoenzyme that catalyzes radical C-C bond cleavages.\n\n\nBiogr
 aphy:\nCathleen Zeymer studied Chemistry at TU Dresden and UC Berkeley. Sh
 e performed her PhD studies in Biochemistry/Biophysics at the Max Planck I
 nstitute for Medical Research in Heidelberg. Cathleen joined ETH Zurich as
  a postdoctoral fellow in 2015 and started an Ambizione-funded junior rese
 arch group in 2019. She was appointed as Tenure Track Assistant Professor 
 for Protein Chemistry at the Technical University of Munich (TUM) in 2020.
 \nSince her diploma thesis\, Cathleen is driven by a passion for enzymes. 
 She is fascinated by the biomolecular structures and mechanisms that enabl
 e such efficient and selective catalysis in proteins. She now wants to tra
 nsfer these principles to the design and evolution of artificial metalloen
 zymes and photoenzymes. Teaching and mentoring students is a matter close 
 to her heart. Cathleen loves to spend her free time hiking or skiing in th
 e mountains.\n\nLab Website:\nwww.bio.nat.tum.de/en/proteinchemie
LOCATION:MED 0 1418 https://plan.epfl.ch/?room==MED%200%201418
STATUS:CONFIRMED
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