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Picosecond Energy Transfer Kinetics in Chlorosomes and Bacteriochlorophyll ,-Proteins of ,In this paper we report a picosecond absorption spectroscopy study of the energy transfer and excited state lifetimes of two Light-harvesting complexes, namely chlorosomes and the BChl a-protein of the green sulfur bacterium . f. . (strain Tassajara).

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Andrzej Moniuszko,B. Adrian Kesala “.553”, which consists of a 47-kDa subunit containing a single covalentty bound FRO and a 11-kDa subunit containing a single heme c (Meyer et al., 1986; Yamanaka, 1976; Yamanaka et al., 1979), has been demonstrated to catalyze electron flow from sulfide to Cyt “.555” (Kusai and Yamanaka, 1973, 1978; Kusai and Fukumori, 1980).

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The Mechanism of Photosynthetic Electron Transport and Energy Transduction by Membrane Fragments fropH 6.1 of + 360 mV whereas a membrane-bound photooxidizable c-type cytochrome (.554) that serves as the electron donor to P870 has its E. 8.1 around + 260 mV. This cytochrome has subsequently been isolated and found to contain two spectrally identical but thermodynamically distinct hemes with E. of