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• W2051212519 abstract "Quantitative electron paramagnetic resonance studies of the primary event associated with Photosystem I in chloroplasts have been carried out at 25 °K. After illumination of either whole chloroplasts or Photosystem I subchloroplast fragments (D-144) with 715-nm actinic light at 25 °K, equal spin concentrations of oxidized P700 and reduced bound iron-sulfur protein (bound ferredoxin) have been measured. Quantitative determination of the concentration of these two carriers by EPR spectroscopy after illumination at low temperature indicates that Photosystem I fragments are enriched in P700 and the bound iron-sulfur protein as compared with unfractionated chloroplasts. These results indicate that P700 and the bound iron-sulfur protein function as the donor-acceptor complex of chloroplast Photosystem I." @default.
• W2051212519 created "2016-06-24" @default.
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• W2051212519 date "1972-12-01" @default.
• W2051212519 modified "2023-10-03" @default.
• W2051212519 title "Quantitative EPR studies of the primary reaction of Photosystem I in chloroplasts" @default.
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• W2051212519 doi "https://doi.org/10.1016/0005-2728(72)90262-9" @default.
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