Analysis of the absorption spectrum of photosystem II reaction centers: temperature dependence, pigment assignment, and inhomogeneous broadening.
In this study a model for decomposition and pigment assignment of the low-temperature (10 K) absorption spectrum of the photosystem II reaction center (D1-D2-cytochrome b559 complex, PSII-RC) is developed. It is based on theoretical calculations of the line shapes of the inhomogeneously broadened pigment spectra, taking into account electron-phonon coupling. The analysis is performed under the hypothesis that exciton coupling is weak, except for the P680 special pair. In this way a detailed decomposition of the absorption spectrum is obtained. Within the model the temperature dependence of the spectrum can be well explained. It is mainly caused by the temperature-dependent changes of the homogeneous absorption spectra of the individual pigments in the PSII-RC. In addition, slight changes in the inhomogeneous distribution functions have to be taken into account. Two slightly different parameter sets are found. We prefer one of these parameter sets which indicates that an accessory chlorophyll (Chl) is the lowest energy pigment in the RC core and that the two antenna Chls have their spectral maxima at 667.7 and 677.9 nm, respectively. The relationship between the shape of the absorption spectrum and the pigment stoichiometry of the sample (ratio of chlorophyll a:pheophytin a), which was noticed by comparison of a variety of different independently prepared samples, can be explained by the presence of "additional" Chl molecules which are nonstoichiometrically bound to part of the PSII-RCs. These Chls can be grouped into three spectrally distinguishable pools. One of them has its absorption maximum at about 683 nm and is responsible for the prominent shoulder that is present in the 10 K absorption spectra of most PSII-RC preparations. Our results suggest that the Chl content of the samples has been underestimated in many spectroscopic studies on the PSII-RC.
Konermann
L
L
Max-Planck-Institut für Strahlenchemie, Mülheim a.d. Ruhr, Germany.
Holzwarth
A R
AR
D002734:Chlorophyll / Q000032:analysis*; D045342:Light-Harvesting Protein Complexes; D010674:Pheophytins / Q000032:analysis*; D045322:Photosynthetic Reaction Center Complex Proteins / Q000032:analysis / Q000737:chemistry*; D045332:Photosystem II Protein Complex; D013053:Spectrophotometry; D013696:Temperature
D045342:Light-Harvesting Protein Complexes; D010674:Pheophytins; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D002734:Chlorophyll; C061694:pheophytin a