| Autor: |
Andersen LH; Department of Physics and Astronomy, Aarhus University, DK-8000 Aarhus C, Denmark., Rasmussen AP; Department of Physics and Astronomy, Aarhus University, DK-8000 Aarhus C, Denmark., Pedersen HB; Department of Physics and Astronomy, Aarhus University, DK-8000 Aarhus C, Denmark., Beletsan OB; Department of Chemistry, Lomonosov Moscow State University, 119991 Moscow, Russia., Bochenkova AV; Department of Chemistry, Lomonosov Moscow State University, 119991 Moscow, Russia. |
| Abstrakt: |
By time-resolved action spectroscopy of cryogenically cooled molecular ions, we have achieved a remarkable vibrational resolution in the photoresponse of the deprotonated green fluorescent protein (GFP) chromophore, a key molecular unit in the bioimaging of living cells. We define four characteristic spectral regions of the S 0 -S 1 band with competing electronic and nuclear decay channels. We determine the energy barrier toward internal conversion to be ∼250 cm -1 . This inhibits internal conversion and hence statistical fragmentation near the S 0 -S 1 band origin, which is identified at 481.51 ± 0.15 nm (20768 ± 6 cm -1 ). The origin is red-shifted by only 221 cm -1 compared to that of wild-type GFP at 77 K. This, together with a striking agreement between the vibronic profiles of the protein and its chromophore, suggests their similar photophysics. In combination with theory, the data reveal the coexistence of mutually energy-borrowing mechanisms between nuclei and electrons mediated by specific vibrational modes. |
