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Subpicosecond Midinfrared Spectroscopy of the P_fr Reaction of Phytochrome Agp1 from Agrobacterium tumefaciens

Christian Schumann ^*, Ruth Groß ^*, Matthias M. N. Wolf ^*, Rolf Diller ^*, Norbert Michael  and Tilman Lamparter 

^* Fachbereich Physik, Technische Universität Kaiserslautern, Kaiserslautern, Germany; and Institut für Pflanzenphysiologie, Freie Universität Berlin, Berlin, Germany

Correspondence: Address reprint requests to Rolf Diller, Tel.: 49-631-205-2323; E-mail: diller{at}physik.uni-kl.de.

Phytochromes are light-sensing pigments found in plants and bacteria. For the first time, the P_fr photoreaction of a phytochrome has been subject to ultrafast infrared vibrational spectroscopy. Three time constants of 0.3 ps, 1.3 ps, and 4.0 ps were derived from the kinetics of structurally specific marker bands of the biliverdin chromophore of Agp1-BV from Agrobacterium tumefaciens after excitation at 765 nm. VIS-pump-VIS-probe experiments yield time constants of 0.44 ps and 3.3 ps for the underlying electronic-state dynamics. A reaction scheme is proposed including two kinetic steps on the S₁ excited-state surface and the cooling of a vibrationally hot P_fr ground state. It is concluded that the upper limit of the E-Z isomerization of the C₁₅ = C₁₆ methine bridge is given by the intermediate time constant of 1.3 ps. The reaction scheme is reminiscent of that of the corresponding P_r reaction of Agp1-BV as published earlier.