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  • energy transfer  (2)
  • 1990-1994  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Studies of excitation energy transfer within the green alga Chlamydomonas reinhardtii and its mutants at 77 K (1991)
    Springer
    Photosynthesis research 27 (1991), S. 157-168 
    Details
    ISSN: 1573-5079
    Keywords: Chlamydomonas reinhardtii ; mutant ; fluorescence ; picosecond ; energy transfer ; light-harvesting complexes (LHC) ; photosystem I (PSI) ; photosystem II (PS II) ; kenetic model
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The 77 K picosecond fluorescence of intact Chlamydomonas reinhardtii exhibits a 680-nm band (F680) that can be identified with light-harvesting chlorophyll. Analysis of the time and spectral dependence of F680 reveal a forward transfer rate of 1/(15 ps) from this 680-nm species to photosystem II. The possibility of transfer through LHC I, the light-harvesting complex closely associated with photosystem I with a transfer time of 60 to 100 ps, is indicated by analysis of similar data in the 700–720 nm region. Simple kinetic models that account for the time dependence of the emissions F707, F703 and F715 are proposed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00035837
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  • 2
    Electronic Resource
    Electronic Resource
    Redox effects on the bacteriochlorophyll α-containing Fenna-Matthews-Olson protein fromChlorobium tepidum (1994)
    Springer
    Photosynthesis research 41 (1994), S. 89-96 
    Details
    ISSN: 1573-5079
    Keywords: photosynthesis ; Chlorobium tepidum ; antenna ; bacteriochlorophylla protein ; energy transfer ; chlorosome ; green bacteria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The BChla-containing Fenna-Matthews-Olson (FMO) protein from the green sulfur bacteriumChlorobium tepidum was purified and characterized. Fluorescence spectra indicate that efficient excited state quenching occurs at neutral or oxidizing redox potentials. The major fluorescence lifetime at room temperature is approximately 60 ps in samples that are in neutral or oxidizing conditions, and approximately 2 ns in samples where the strong reductant sodium dithionite has been added. A similar change is observed in pump-probe picosecond absorbance difference experiments, where the long life time component increases after dithionite addition. A 16 Gauss wide EPR signal with g factor =2.005 is observed in samples without dithionite. This signal largely disappears upon addition of dithionite. Dithionite induces large reversibile changes in the 77 K absorbance spectra of the purified FMO protein and in whole cells. These results indicate that the FMO protein contains redox active groups, which may be involved in the regulation of energy transfer. Room temperature circular dichroism and low temperature absorption spectra show that dithionite also induces conformational or structural changes of the FMO protein complex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02184148
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    Paper (German National Licenses)
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