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Titlebook: Current topics in photosynthesis; Dedicated to Profess J. Amesz,A. J. Hoff,H. J. Gorkum Book 1986 Martinus Nijhoff Publishers, Dordrecht 19

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Oxidation of cytochrome ,, by photosynthetic reaction centers of , and , in vivo. Effect of viscositIn . and . it is shown that the oxidation of cytochrome .. involves a diffusion limited process. From analysis of the results it follows that the electron transfer probability must be very low. This is corroborated by in vitro studies using the isolated components.
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Molecular arrangement of pigment-protein complex of photosystem 1 chlorophyll content. Chlorophyll seems to be grouped in clusters (5–7 molecules) in the hydrophobic cores of 2–3 parallel . domains of the 65 kDa protein. Only one of the clusters in CP1-RC includes P700; on P700 photooxidation the change of its interaction with the nearest pigment environment resu
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Triplet-minus-singlet absorbance difference spectra of reaction centers of , R-26 in the temperatureo shifting bands in the 800 nm region are identified as the two bands at 803 and 813 nm which together make up the 800 nm band in the absorption spectrum and are assigned to the two accessory RC bacteriochlorophylls (BChls). The band shift of the 813 nm pigment is appreciably larger than that of the
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ESR spectroscopy demonstrates that cytochrome b559 remains low potential in Ca2+-reactivated, salt-wential form(s) to those of lower potential. Exposure of the membranes to 2 M NaCl shifts a significant amount of high potential cyt b. to lower potential form(s); addition of CaCl. reconstituted oxygen evolution activity but did not restore cyt b. to its high potential form(s).
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