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À propos de : Spectroscopy and Photochemistry of Spinach Photosystem IEntrapped and Stabilized in a Hybrid Organosilicate Glass        

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  • Spectroscopy and Photochemistry of Spinach Photosystem IEntrapped and Stabilized in a Hybrid Organosilicate Glass
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  • Photosystem I (PSI) is part of the photosynthetic apparatus of higher plants and algae. It is one of thenaturally occurring molecular photovoltaic structures whose primary function is to convert solar energyinto chemical energy. The immobilization and stabilization of this large transmembrane protein complexin a solvent-limited and optically clear organosilicate glass are reported. This was achieved by amodification of the sol-gel process whereby in the first instance the methanol formed during the hydrolysisof the alkoxide precursor was removed before adding the enzyme preparation. In the second instance,glycerol was used as a nonsurfactant templating agent. It was present at a final concentration of 50%(v/v) after the solvent removal process was completed. In addition to stabilizing PSI, it may also play animportant structural role, as its omission results in opaque and brittle glasses. The PSI complexes retainedtheir activity during the immobilization procedure and after 96% (w/w) of the solvent in the sol-gelmatrix was removed. The ability of the P700 reaction centers in entrapped PSI to undergo photochemicaloxidation indicated that the intramolecular electron-transfer apparatus of the reaction centers was functional.In addition, it was demonstrated that their intermolecular electron-transfer function was also intact, asevidenced by PSI-mediated photodependent hydrogen production. The results demonstrate the validityof this novel approach for investigation of complex biological electron-transfer processes under nonnativeconditions.
  • Photosystem I isolated from spinach was immobilized and stabilized in a solvent-limited optically clear organo-silicate glass. Removal of methanol and addition of glycerol as a templating agent protected the protein from denaturation. The intra- and intermolecular electron-transfer pathways of the immobilized protein were preserved during entrapment and subsequent dehydration.
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