De novo lanthanide enzymes – from protein dynamics to photoredox catalysis +CH636
Event details
| Date | 14.05.2024 |
| Hour | 16:15 › 17:15 |
| Speaker | Cathleen Zeymer |
| Location | |
| Category | Conferences - Seminars |
| Event Language | English |
Abstract:
A major challenge in biocatalysis is the development of novel enzymes for reactions beyond nature’s synthetic repertoire. Our approach combines rational design and directed evolution to generate artificial metalloenzymes and photoenzymes. We recently reported a de novo protein scaffold with femtomolar affinity for lanthanide ions. These metal cofactors are not only potent Lewis acid catalysts, some of them also promote photoredox chemistry. We have been characterizing the interplay between functional protein dynamics and metal coordination in these systems with various biophysical techniques and developed a cerium-dependent photoenzyme that catalyzes radical C-C bond cleavages.
Biography:
Cathleen Zeymer studied Chemistry at TU Dresden and UC Berkeley. She performed her PhD studies in Biochemistry/Biophysics at the Max Planck Institute for Medical Research in Heidelberg. Cathleen joined ETH Zurich as a postdoctoral fellow in 2015 and started an Ambizione-funded junior research group in 2019. She was appointed as Tenure Track Assistant Professor for Protein Chemistry at the Technical University of Munich (TUM) in 2020.
Since her diploma thesis, Cathleen is driven by a passion for enzymes. She is fascinated by the biomolecular structures and mechanisms that enable such efficient and selective catalysis in proteins. She now wants to transfer these principles to the design and evolution of artificial metalloenzymes and photoenzymes. Teaching and mentoring students is a matter close to her heart. Cathleen loves to spend her free time hiking or skiing in the mountains.
Lab Website:
www.bio.nat.tum.de/en/proteinchemie
A major challenge in biocatalysis is the development of novel enzymes for reactions beyond nature’s synthetic repertoire. Our approach combines rational design and directed evolution to generate artificial metalloenzymes and photoenzymes. We recently reported a de novo protein scaffold with femtomolar affinity for lanthanide ions. These metal cofactors are not only potent Lewis acid catalysts, some of them also promote photoredox chemistry. We have been characterizing the interplay between functional protein dynamics and metal coordination in these systems with various biophysical techniques and developed a cerium-dependent photoenzyme that catalyzes radical C-C bond cleavages.
Biography:
Cathleen Zeymer studied Chemistry at TU Dresden and UC Berkeley. She performed her PhD studies in Biochemistry/Biophysics at the Max Planck Institute for Medical Research in Heidelberg. Cathleen joined ETH Zurich as a postdoctoral fellow in 2015 and started an Ambizione-funded junior research group in 2019. She was appointed as Tenure Track Assistant Professor for Protein Chemistry at the Technical University of Munich (TUM) in 2020.
Since her diploma thesis, Cathleen is driven by a passion for enzymes. She is fascinated by the biomolecular structures and mechanisms that enable such efficient and selective catalysis in proteins. She now wants to transfer these principles to the design and evolution of artificial metalloenzymes and photoenzymes. Teaching and mentoring students is a matter close to her heart. Cathleen loves to spend her free time hiking or skiing in the mountains.
Lab Website:
www.bio.nat.tum.de/en/proteinchemie
Practical information
- Informed public
- Free