9 research outputs found

    Site-directed mutations at D1-His198 and D1-Thr179 of photosystem II in Synechocystis sp. PCC 6803: deciphering the spectral properties of the PSII reaction centre

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    Site-directed mutations were constructed in photosystem II of Synechocystis sp. PCC6803 in which the axial ligand, D1-His198, of special pair chlorophyll PD1 was replaced with Gln and where D1-Thr179, which overlies monomeric chlorophyll ChlD1, was replaced with His. The D1-His198Gln mutation produces a 3 nm displacement to the blue of the bleaching minimum in the Soret and in the Qy region of the (P+QA−–PQA) absorbance difference spectrum. To a first approximation, the bleaching can be assigned to the low-energy exciton transition of the special pair chlorophylls PD1/PD2. The D1-Thr179His mutation produces a 2 nm displacement to the red of the bleaching minimum in the Qy region of the (3P–1P) absorbance difference spectrum. Analysis of the flash-induced (P+QA−–PQA) and (3P–1P) absorbance difference spectra of both mutants compared with wild-type at 80 K indicate that the cation of the oxidized donor P+ is predominantly localized on the chlorophyll PD1 of the special pair and that the reaction centre triplet state, produced upon charge recombination from 3[P+Pheo−], when the primary quinone electron acceptor QA is doubly reduced, is primarily localized on ChlD1

    The Pathway, Kinetics and Thermodynamics of Electron Transfer in Wild Type and Mutant Reaction Centers of Purple Nonsulfur Bacteria

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    The Recombination Dynamics of the Radical Pair P+H− in External Magnetic and Electric Fields

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    Immunohistochemical Analysis of Matrix Proteolytic Enzymes in the Periprosthetic Tissue in the Patients with Loosening Prostheses.

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    Concentration of Metal Elements in the Blood and Urine in the Patients with Cementless Total Knee Arthroplasty.

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    Pathophysiology of the enterohepatic circulation of bile acids

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