| Picosecond dynamics of primary electron-transfer processes in bacterial photosynthesis Biophysical Journal, Volume 23, Issue 2, 1 August 1978, Pages 207-217 K. Peters, P. Avouris and P.M. Rentzepis Abstract The primary electron transfer processes in Rhodopseudomonas sphaeroides R-26 were studied as a function of temperature by means of picosecond spectroscopy. The first chemical step of the bacterial photosynthesis involves an electron transfer from the excited state of a bacteriochlorophyll a dimer, (BChl)2, to a bacteriopheophytin (BPh) to form the radical ion pair (BChl)2+. BPh-. The upper limit for the formation time of this ion-pair was found to be 10 ps, at temperatures in the range 300–4.2 degree K. Similarly, the second chemical step, involving electron transfer from BPh-. to an ubiquinone-iron complex (QFe), was found to have a lifetime of approximately 150 ps, also independent of temperature in the same range. We interpret the absence of temperature dependence as indicating that process 2 proceeds via a tunneling mechanism. Utilizing our results in conjunction with electron tunneling theories, we calculate the distance between BPh-. and Q(Fe) to be 9--13 A. Our results also imply a closer proximity between (BChl)2 and BPh. Abstract | PDF (605 kb) |
| B800→B850 Energy Transfer Mechanism in Bacterial LH2 Complexes Investigated by B800 Pigment Exchange Biophysical Journal, Volume 78, Issue 5, 1 May 2000, Pages 2590-2596 J.L. Herek, N.J. Fraser, T. Pullerits, P. Martinsson, T. Polívka, H. Scheer, R.J. Cogdell and V. Sundström Abstract Femtosecond transient absorption measurements were performed on native and a series of reconstituted LH2 complexes from 10050 at room temperature. The reconstituted complexes contain chemically modified tetrapyrrole pigments in place of the native bacteriochlorophyll -B800 molecules. The spectral characteristics of the modified pigments vary significantly, such that within the B800 binding sites the B800 absorption maximum can be shifted incrementally from 800 to 670nm. As the spectral overlap between the B800 and B850 bands decreases, the rate of energy transfer (as determined by the time-dependent bleaching of the B850 absorption band) also decreases; the measured time constants range from 0.9ps (bacteriochlorophyll in the B800 sites, absorption maximum at 800nm) to 8.3ps (chlorophyll in the B800 sites, absorption maximum at 670nm). This correlation between energy transfer rate and spectral blue-shift of the B800 absorption band is in qualitative agreement with the trend predicted from Förster spectral overlap calculations, although the experimentally determined rates are ∼5 times faster than those predicted by simulations. This discrepancy is attributed to an underestimation of the electronic coupling between the B800 and B850 molecules. Abstract | Full Text | PDF (133 kb) |
| Photochemical Electron Transport in Photosynthetic Reaction Centers Biophysical Journal, Volume 12, Issue 10, 1 October 1972, Pages 1221-1234 Roderick K. Clayton and Susan C. Straley Abstract The formation and dissipation of reduced photoproducts in photochemical reaction centers from has been studied in three independent ways: by direct chemical reduction, by photochemical reduction (illuminating reaction centers in the presence of weak reductants), and by adding electron acceptors to illuminated reaction centers to reverse the reduction. In every case the reduction is attended by the appearance of an absorption band at 450 nm and the bathochromic shift of a band centered at 305 nm. Both reduction and oxidation of reaction centers, and also photochemical oxidoreduction, cause bathochromic shifts of absorption bands identified with bacteriopheophytin (BPh), and hypsochromic shifts of bands of bacteriochlorophyll (BChl) (P-800 and, in the case of reduction, P-870). Reduction causes relatively large shifts of BPh and small shifts of BChl; the reverse is seen with oxidation and oxidoreduction. Addition of sodium dodecyl sulfate (SDS) to reaction centers suppresses the 450 nm absorption change but not the band shifts associated with BPh and BChl. Under some conditions the 450 nm change and the band shifts show different kinetics, with the kinetics of the band shifts matching those of a transient change in the yield of P-870 fluorescence. New data, on the efficiency of photo-bleaching of P-870 in reaction centers in which part of the P-870 has already been oxidized with ferricyanide, militate against the idea that part of the photochemical bleaching of P-870 is due to reduction of that pigment. Abstract | PDF (736 kb) |
Copyright © 1982 The Biophysical Society. All rights reserved.
Biophysical Journal, Volume 39, Issue 1, 91-99, 1 July 1982
doi:10.1016/S0006-3495(82)84494-9
Research Article
A. Ogrodnik, H.W. Krüger, H. Orthuber, R. Haberkorn, M.E. Michel-Beyerle and H. Scheer
The time dependence of magnetic field effects on light absorption by triplet-state and radical ions in quinone-depleted reaction centers of Rhodopseudomonas sphaeroides strain R-26 has been investigated. Measurements on the time scale of the hyperfine interaction in the radical pair [(BChl)2+. ...BPh-.)] provided kinetic data characterizing the recombination process. The results have been interpreted in terms of a recently proposed model that assumes an intermediate electron acceptor (close site) between the bacteriochlorophyll "special pair" (BChl)2 and the bacteriopheophytin BPh (distant site). Recombination is assumed to proceed through this intermediate acceptor. The experiments led to effective recombination rates for the singlet and triplet channel: k(Seff) = 3.9 . 107 s-1 and k(Teff) = 7.4 . 10(8) s-1. These correspond to recombination rates ks = 1 . 10(1) s-1 and kT = 7.1 . 10(11) s-1 in the close configuration. The upper bound of the effective spin dephasing rate k2eff approximately equal to 1 . 10(9) s-1 is identical with the rate of the electron hopping between the distant site of zero spin exchange interaction and the close site of large interaction. Interpretation of data for the case of direct recombination yields the recombination rates, spin dephasing rate, and exchange interaction in a straightforward way.