dc.creatorYang, Yang
dc.creatorLinke, Martin
dc.creatorvon Haimberger, Theodore
dc.creatorHahn, Janina
dc.creatorMatute Morales, Ricardo
dc.creatorGonzález, Leticia
dc.creatorSchmieder, Peter
dc.creatorHeyne, Karsten
dc.date.accessioned2012-08-01T15:37:18Z
dc.date.available2012-08-01T15:37:18Z
dc.date.created2012-08-01T15:37:18Z
dc.date.issued2012
dc.identifierJOURNAL OF THE AMERICAN CHEMICAL SOCIETY Volume: 134 Issue: 3 Pages: 1408-1411 Published: JAN 25 2012
dc.identifierDOI: 10.1021/ja209413d
dc.identifierhttps://repositorio.uchile.cl/handle/2250/119532
dc.description.abstractPhotoisomerization 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.languageen
dc.publisherAMER CHEMICAL SOC
dc.subjectSUBPICOSECOND MIDINFRARED SPECTROSCOPY
dc.titleReal-Time Tracking of Phytochrome's Orientational Changes During Pr Photoisomerization
dc.typeArtículo de revista


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