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VH-NG-1502
Role of Enzyme Dynamics in Catalysis Revealed by Time Resolved Crystallography
| Coordinator | Lane, Thomas ; Pearson, Arwen |
| Grant period | 2020-2026 |
| Funding body | Helmholtz Gemeinschaft Deutscher Forschungszentren |
| HGF | |
| Identifier | G:(DE-HGF)2020_VH-NG-1502 |
⇧ Impuls- und Vernetzungsfonds ⇧
Note: Enzymes are biology’s machines for doing chemistry. In addition to being central to life as we know it, they often perform desirable reactions many orders of magnitude faster than man-made catalysts with stereoselectivity and specificity. Yet a full physical description of how this is possible is lacking. As a result, we do not fully understand life and our ability to create new enzymes is limited. I propose to address this knowledge gap by imaging enzymes while they perform catalysis. Since chemistry involves the rearrangement of bonds, imaging of such processes requires atomic spatial resolution and femtosecond temporal resolution, only recently possible thanks to X-ray free electron lasers like the European XFEL. Such experiments require initiation of the enzyme reaction with femtosecond temporal resolution, currently only possible using ultrafast lasers. Therefore, we will first study one of the few naturally light-triggered enzymes, DNA photolyase, which conducts a DNA repair reaction. Simultaneously, we will pursue the development of a light-activated enzyme cofactor, a photoNAD(P)H. This will enable us to turn the drug target DHFR into a light-activated system, allowing us to image it, resolving open questions about how it functions while demonstrating the new photoNAD(P)H technology.Recent Publications
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Record created 2020-10-20, last modified 2020-10-20
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