Photoactive Yellow Protein – Converting Light into a Metastable Structural Change
Event details
| Date | 23.10.2014 |
| Hour | 16:30 › 17:30 |
| Speaker |
Prof. Marloes Groot VU University, Amsterdam |
| Location | |
| Category | Conferences - Seminars |
Two questions at the forefront of biophysical sciences are biological sensing and energy conversion. Photoactive Yellow Protein is at the cross point of these two topics as it converts light energy into a structural change, in the process of biological light sensing. This bacterial photosensor is an excellent model system to study how a protein achieves such a function as it is relatively small and very stable.
Biological signal transduction by photoactive yellow protein (PYP) in halophilic purple sulfur bacteria is initiated by trans-to-cis isomerization of the p-coumaric acid chromophore (pCa) of PYP. pCa is engaged in two short hydrogen bonds with protein residues E46 and Y42, a normal hydrogen bond with Cys69 and it is negatively charged at the phenolate oxygen. We have applied ultrafast pump-probe spectroscopy in the visible and midinfrared spectral regions to study the rate and quantum yield of the isomerization process, and the role of the three hydrogen bonds and the role of local charges in the formation of the stable long-lived isomer.
Biological signal transduction by photoactive yellow protein (PYP) in halophilic purple sulfur bacteria is initiated by trans-to-cis isomerization of the p-coumaric acid chromophore (pCa) of PYP. pCa is engaged in two short hydrogen bonds with protein residues E46 and Y42, a normal hydrogen bond with Cys69 and it is negatively charged at the phenolate oxygen. We have applied ultrafast pump-probe spectroscopy in the visible and midinfrared spectral regions to study the rate and quantum yield of the isomerization process, and the role of the three hydrogen bonds and the role of local charges in the formation of the stable long-lived isomer.
Practical information
- General public
- Free
Organizer
- Dr Frank van Mourik