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- W2368800565 abstract "During the last few years a number of significant advances have been made in the knowledge of the structure-function relationship of photosystem Ⅱ. Recent studies suggested that the site for the primary photochemistry in PS Ⅱ was located on the D1 and D2 proteins. However, the D1 / D2 / Cyt b559 complex conrained no plastoquinone or Mn. In this paper, a photosystem Ⅱ reaction center complex consisting of 47 kD, D1 and D2 polypeptides and cytochrome b-559 (Fig. 2) was isolated from spinach grana thylakoids by treating with 4% Triton X-100 in the presence of ascorbate and glycerol at acidic pH, followed by ionexchange chromatographic separation using DEAE-Toyopearl 650S. The isolated complex was fairly active in the DCIP photoreduction with DPC (190 μ electron eqivalents per mg chlorophyll per h) (Fig. 5) and exhibited a dark-stable and photo-induced EPR Signal Ⅱ (Fig. 8). The absorption (Fig. 3, 4), fluorescence (Figs 6, 7) spectral properties of 47 kD/ /D1/D2/Cyt b559 indicate that only Chl a is present. The Chi a / Pheo a / Cyt b559 /Mn molar ratio in the complex is 18.4:2.0:0.8:0.3. These results suggest that the protein complex contains the intact PS Ⅱ elecotron transport chain from the secondary electron donor Z to the primary electron acceptor Q_A, and also indicate the possibility that Mnbinding site is located in the protein complex. It provides an evidence for the view that the principal site of water oxidation is associated with the PSⅡ reaction center complex (Tang and Satoh 1985)." @default.
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- W2368800565 date "1992-01-01" @default.
- W2368800565 modified "2023-09-26" @default.
- W2368800565 title "Isolation and Characterization of a 47 kD/D1/D2/cytochrome b559 Reaction Center Complex of Photosystem I from Spinach" @default.
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