dc.creator | Yang, Yang | |
dc.creator | Linke, Martin | |
dc.creator | von Haimberger, Theodore | |
dc.creator | Hahn, Janina | |
dc.creator | Matute Morales, Ricardo | |
dc.creator | González, Leticia | |
dc.creator | Schmieder, Peter | |
dc.creator | Heyne, Karsten | |
dc.date.accessioned | 2012-08-01T15:37:18Z | |
dc.date.available | 2012-08-01T15:37:18Z | |
dc.date.created | 2012-08-01T15:37:18Z | |
dc.date.issued | 2012 | |
dc.identifier | JOURNAL OF THE AMERICAN CHEMICAL SOCIETY Volume: 134 Issue: 3 Pages: 1408-1411 Published: JAN 25 2012 | |
dc.identifier | DOI: 10.1021/ja209413d | |
dc.identifier | https://repositorio.uchile.cl/handle/2250/119532 | |
dc.description.abstract | Photoisomerization of a protein bound chromophore is the basis of the light sensing and signaling responses of many photoreceptors. Z-to-E photoisomerization of the Pr Cph1 Delta 2 phytochrome has been investigated by polarization resolved femtosecond visible pump-infrared probe spectroscopy, which yields structural information on the Pr excited (Pr*), Pr ground, and lumi-R product states. By exhaustive search analysis, two photoreaction time constants of (4.7 +/- 1.4) and (30 +/- 5) ps were found. Ring D orientational change in the electronic excited state to the transition state (90 degrees twist) has been followed in real-time. Rotation of ring D takes place in the electronically excited state with a time constant of 30 +/- 5 ps. The photoisomerization is best explained by a single rotation around C-15=C-16 methine bridge in the Pr* state and a diffusive interaction with its protein surrounding. | |
dc.language | en | |
dc.publisher | AMER CHEMICAL SOC | |
dc.subject | SUBPICOSECOND MIDINFRARED SPECTROSCOPY | |
dc.title | Real-Time Tracking of Phytochrome's Orientational Changes During Pr Photoisomerization | |
dc.type | Artículo de revista | |