| Spectral Inhomogeneity of Photosystem I and Its Influence on Excitation Equilibration and Trapping in the Cyanobacterium Synechocystis sp. PCC6803 at 77 K Biophysical Journal, Volume 81, Issue 2, 1 August 2001, Pages 1144-1154 Alexander N. Melkozernov, Su Lin, Robert E. Blankenship and Leonas Valkunas Abstract Ultrafast transient absorption spectroscopy was used to probe excitation energy transfer and trapping at 77K in the photosystem I (PSI) core antenna from the cyanobacterium PCC 6803. Excitation of the bulk antenna at 670 and 680nm induces a subpicosecond energy transfer process that populates the Chl spectral form at 685–687nm within few transfer steps (300–400 fs). On a picosecond time scale equilibration with the longest-wavelength absorbing pigments occurs within 4–6ps, slightly slower than at room temperature. At low temperatures in the absence of uphill energy transfer the energy equilibration processes involve low-energy shifted chlorophyll spectral forms of the bulk antenna participating in a 30–50-ps process of photochemical trapping of the excitation by P. These spectral forms might originate from clustered pigments in the core antenna and coupled chlorophylls of the reaction center. Part of the excitation is trapped on a pool of the longest-wavelength absorbing pigments serving as deep traps at 77K. Transient hole burning of the ground-state absorption of the PSI with excitation at 710 and 720nm indicates heterogeneity of the red pigment absorption band with two broad homogeneous transitions at 708nm and 714nm (full-width at half-maximum (fwhm) ∼ 200–300cm). The origin of these two bands is attributed to the presence of two chlorophyll dimers, while the appearance of the early time bleaching bands at 683nm and 678nm under excitation into the red side of the absorption spectrum (>690nm) can be explained by borrowing of the dipole strength by the ground-state absorption of the chlorophyll monomers from the excited-state absorption of the dimeric red pigments. Abstract | Full Text | PDF (218 kb) |
| Two-Photon Absorption of Bacteriorhodopsin: Formation of a Red-Shifted Thermally Stable Photoproduct F620 Biophysical Journal, Volume 89, Issue 2, 1 August 2005, Pages 1175-1182 Thorsten Fischer and Norbert A. Hampp Abstract By means of high-intensity 532nm laser pulses, a photochemical conversion of the initial B state of bacteriorhodopsin (BR) to a stable photoproduct absorbing maximally at ≈620nm in BR suspensions and at ≈610nm in BR films is induced. This state, which we named F, is photochemically further converted to a group of three products with maximal absorptions in the wavelength range from 340nm to 380nm, which show identical spectral properties to the so-called P state reported in the literature. The photoconversion from B to F is most likely a resonant two-photon absorption induced step. The formation of F and P leads to a distinguished photo-induced permanent optical anisotropy in BR films. The spectral dependence of the photo-induced anisotropy and the anisotropy orientations at the educt (B) and product (F) wavelengths are strong indicators that F is formed in a direct photochemical step from B The chemical nature of the P products probably is that of a retro-retinal containing BR, but the structural characteristics of the F state are still unclear. The photo-induced permanent anisotropy induced by short laser pulses in BR films helps to better understand the photochemical pathways related to this transition, and it is interesting in view of potential applications as this feature is the molecular basis for permanent optical data storage using BR films. Abstract | Full Text | PDF (189 kb) |
| Femtosecond Spectroscopic Observations of Initial Intermediates in the Photocycle of the Photoactive Yellow Protein from Ectothiorhodospira halophila Biophysical Journal, Volume 77, Issue 2, 1 August 1999, Pages 1017-1023 Savitha Devanathan, Andrew Pacheco, Laszlo Ujj, Michael Cusanovich, Gordon Tollin, Su Lin and Neal Woodbury Abstract Femtosecond time-resolved absorbance measurements were used to probe the subpicosecond primary events of the photoactive yellow protein (PYP), a 14-kD soluble photoreceptor from . Previous picosecond absorption studies from our laboratory have revealed the presence of two new early photochemical intermediates in the PYP photocycle, I, which appears in ≤3ps, and I, which is formed in 220ps, as well as stimulated emission from the PYP excited state. In the present study, kinetic measurements at two excitation wavelengths (395nm and 460nm) on either side of the PYP absorption maximum (446nm) were undertaken using 100-fs pump and probe pulses. Global analysis over a range of probe wavelengths yielded time constants of 1.9ps for the photochemical formation of the I intermediate via the PYP excited state, and 3.4ps for the repopulation of the ground state from the excited state. In addition to these pathways, 395nm excitation also initiated an alternative route for PYP excitation and photochemistry, presumably involving a different excited electronic state of the chromophore. No photochemical intermediates formed before I were observed. Based on these data, a quantum yield of 0.5–0.6 for I formation was determined. The structural and mechanistic aspects of these results are discussed. Abstract | Full Text | PDF (164 kb) |
Copyright © 1974 The Biophysical Society. All rights reserved.
Biophysical Journal, Volume 14, Issue 6, 490-512, 1 June 1974
doi:10.1016/S0006-3495(74)85929-1
Articles
B. Minke, S. Hochstein and P. Hillman
A “complete” and quantitative kinetic model for the states and transitions of the barnacle visual pigment in situ has been constructed from intracellular recordings of the early receptor potential responses to long light pulses. The model involves two stable and four thermolabile states and 10 photochemical, thermal, and metabolic transitions among them. The existence of each state and transition is demonstrated by qualitative examination of the response resulting from a carefully chosen experimental paradigm (combination of intensity, duration, and wavelength of adaptation and stimulation). Quantitative examination of the same responses determines all of the model transition rates, but only puts constraints on the state dipole moments. The latter are determined, and the former refined, by quantitative comparison of the predictions of the complete model with the responses to a set of paradigms chosen to involve as many states and transitions as possible. The fact that good fits can be obtained to these responses without further modification of the model supports its completeness.