[Electrochemical regulation of the transfer of excitation energy in chlorophyll-protein complexes].
Red absorption band and fluorescence of an artificial chlorophyll-albumin complex (MW 220 kD) resemble the spectroscopic properties of P 680 shifts toward longer waves with the solution pH from 7.3 to 2.5. It is suggested that light induced pH under in vivo conditions may cause similar changes which may lead to changes in the distribution of excitation energy within the pigment system of photosynthesizing organisms.
D002734:Chlorophyll; D003580:Cytochromes; D004563:Electrochemistry; D004735:Energy Transfer; D006863:Hydrogen-Ion Concentration; D045342:Light-Harvesting Protein Complexes; D008081:Liposomes; D010713:Phosphatidylcholines; D010788:Photosynthesis; D045322:Photosynthetic Reaction Center Complex Proteins; D010940:Plant Proteins; D012709:Serum Albumin; D013050:Spectrometry, Fluorescence; D013057:Spectrum Analysis
D003580:Cytochromes; D045342:Light-Harvesting Protein Complexes; D008081:Liposomes; D010713:Phosphatidylcholines; D045322:Photosynthetic Reaction Center Complex Proteins; D010940:Plant Proteins; D012709:Serum Albumin; D002734:Chlorophyll
Elektrokhimicheskaia reguliatsiia perenosa énergii vozbuzhdeniia v kholorofill-belkovykh kompleksakh.