Abstract
Phytochromes are light-sensing pigments found in plants and bacteria. For the first time, the Pfr photoreaction of a phytochrome has been subject to ultrafast infrared vibrational spectroscopy. Three time constants of 0.3ps, 1.3ps, and 4.0ps were derived from the kinetics of structurally specific marker bands of the biliverdin chromophore of Agp1-BV from Agrobacterium tumefaciens after excitation at 765nm. VIS-pump-VIS-probe experiments yield time constants of 0.44ps and 3.3ps 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 Pfr 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 1.3ps. The reaction scheme is reminiscent of that of the corresponding Pr reaction of Agp1-BV as published earlier.
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