Energy transfer and trapping in the photosystem I core antenna. A temperature study.
The fluorescence decay kinetics of the photosystem I-only mutant strain of Chlamydomonas reinhardtii, A4d, are used to study energy transfer and structural organization in photosystem I (PSI). Time-resolved measurements over a wide temperature range (36-295 K) have been made both on cells containing approximately 65 core chl a/P700 and an additional 60-70 chl a + b from LHC proteins and on PSI particles containing 40-50 chl a/P700. In each case, the fluorescence decay kinetics is dominated by a short component, tau 1 which is largely attributed to the lifetime of the excitations in the core complex. The results are discussed in terms of simulations of the temperature dependence of tau 1 in model systems. Spectral inhomogeneity and the temperature dependence of the spectral lineshapes are included explicitly in the simulations. Various kinds of antenna arrangements are modeled with and without the inclusion of pigments with lower absorption energies than the trap (red pigments). We conclude that funnel arrangements are not consistent with our measurements. A random model that includes one or two red pigments placed close to the trap shows temperature and wavelength dependence similar to that observed experimentally. A comparison of the temperature dependence of tau 1 for cells and PSI particles is included.
Werst
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Department of Chemistry, University of Chicago, Illinois 60637.
Jia
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Fleming
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D000818:Animals; D055592:Biophysical Phenomena; D001703:Biophysics; D016825:Chlamydomonas reinhardtii / Q000235:genetics / Q000378:metabolism; D004735:Energy Transfer; D008954:Models, Biological; D009154:Mutation; D045322:Photosynthetic Reaction Center Complex Proteins / Q000235:genetics / Q000378:metabolism* / Q000528:radiation effects; D045331:Photosystem I Protein Complex; D013050:Spectrometry, Fluorescence; D013696:Temperature
D045322:Photosynthetic Reaction Center Complex Proteins; D045331:Photosystem I Protein Complex