Subpicosecond midinfrared spectroscopy of the Pfr reaction of phytochrome Agp1 from Agrobacterium tumefaciens.
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 S(1) 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 C(15) = C(16) 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.
Schumann
Christian
C
Fachbereich Physik, Technische Universität Kaiserslautern, Kaiserslautern, Germany.
Gross
Ruth
R
Wolf
Matthias M N
MM
Diller
Rolf
R
Michael
Norbert
N
Lamparter
Tilman
T
D016960:Agrobacterium tumefaciens / Q000737:chemistry*; D003198:Computer Simulation; D007700:Kinetics; D008027:Light; D008956:Models, Chemical; D010834:Phytochrome / Q000737:chemistry* / Q000528:radiation effects*; D011487:Protein Conformation / Q000528:radiation effects; D013055:Spectrophotometry, Infrared / Q000379:methods*
D010834:Phytochrome