The surface pressure-area (π-A) isotherm of R-phycoerythrin (R-PE) at the air-water interface has been measured. The results indicate that R-PE can form the monomolecular film. Moreover, the molecule-occupied area ex...The surface pressure-area (π-A) isotherm of R-phycoerythrin (R-PE) at the air-water interface has been measured. The results indicate that R-PE can form the monomolecular film. Moreover, the molecule-occupied area extrapolating the linear part of the n-A isotherm is identical with that when an R-PE molecule is located at the interface with its disk plane parallel to the air-water interface. The transmission electron micrograph (TEM) and the measurement of the thickness of the protein monolayer by ellipsometry show that the orientation of R-PE disk plane on the substrate is parallel to the plane of substrate. Absorption and fluorescence spectra of R-PE LB multilayers were obtained through transferring R-PE monolayer at the air-water interface to the substrates at the proper surface pressure by Langmuir-Blodgett (LB) technique. These spectra of R-PE LB films do not show distinct differences from those in aqueous solution. Comparative studies of circular dichroism (CD) spectra of the protein between in展开更多
The antenna system of photosynthetic organisms serves to absorb light energy andtransfer excitation energy to the reaction centers. Energy transfer in the antenna system hasbeen found to be very efficient and rapid. T...The antenna system of photosynthetic organisms serves to absorb light energy andtransfer excitation energy to the reaction centers. Energy transfer in the antenna system hasbeen found to be very efficient and rapid. The overall transfer efficiency exceeds 90％, andthe whole process of energy transfer from the phycoerythrin (PE) to the reaction center iscompleted within 50 ps in intact cells of red algae and cyanobacteria. Phycobilisome. the important photosynthetic antenna in red algae and cyanobacteria,consists of antenna polypeptide rods and core. One side of the core attaches to thethylakoid membrane and connects with the reaction center. the other side connects with展开更多
Through an electrochemical cell deposited with R-phycoerythrin (R-PE) monolayer on SnO2 optically transparent electrode (SnO2 OTE), charge transport phenomenon and the photoelectrochemical behavior of R-PE have been i...Through an electrochemical cell deposited with R-phycoerythrin (R-PE) monolayer on SnO2 optically transparent electrode (SnO2 OTE), charge transport phenomenon and the photoelectrochemical behavior of R-PE have been investigated. The experimental results indicate that the cell is able to generate photocurrent; moreover, the signal increases apparently in the presence of electron donor or acceptor in the electrolyte solution, showing that the photocurrent of R-PE would originate from its charge transfer. Further comparative test showed that the photocurrent came from the photo-induced charge separation property of the chromorphores attached covalently to the apoprotein of R-PE. The photocurrent spectrum of R-PE LB films verified the above viewpoint, from which the mechanism of photo-induced charge transfer of R-PE is suggested. The quantum yield for photoelectric conversion of R-PE LB films was measured to be φ520nm=3.4% and the photovoltage approached 400 mV. Moreover, the protein is stable for a展开更多
Polysiphonia urceolata R phycoerythrin and Porphyridium cruentum B phycoerythrin were degraded with proteinaseK, and then the nearly native γ subunits were isolated from the reaction mixture. The process of degradati...Polysiphonia urceolata R phycoerythrin and Porphyridium cruentum B phycoerythrin were degraded with proteinaseK, and then the nearly native γ subunits were isolated from the reaction mixture. The process of degradation of phycoerythrin with proteinaseK showed that the γ subunit is located in the central cavity of (αβ) 6 hexamer of phycoerythrin. Comparative analysis of the spectra of the native phycoerythrin, the phycoerythrin at pH 12 and the isolated γ subunit showed that the absorption peaks of phycoerythrobilins on α or β subunit are at 535 nm (or 545 nm) and 565 nm, the fluorescence emission maximum at 580 nm; the absorption peak of phycoerythrobilins on the isolated γ subunit is at 589 nm, the fluorescence emission peak at 620 nm which overlaps the absorption maximum of C phycocyanin and perhaps contributes to the energy transfer with high efficiency between phycoerythrin and phycocyanin in phycobilisome; the absorption maximum of phycourobilin on the isolated γ subunit is at 498 nm, which is the same as that in native phycoerythrin, and the fluorescence emission maximum at 575 nm.展开更多
基金Project supported by the National Natural Science Foundation of China
文摘The surface pressure-area (π-A) isotherm of R-phycoerythrin (R-PE) at the air-water interface has been measured. The results indicate that R-PE can form the monomolecular film. Moreover, the molecule-occupied area extrapolating the linear part of the n-A isotherm is identical with that when an R-PE molecule is located at the interface with its disk plane parallel to the air-water interface. The transmission electron micrograph (TEM) and the measurement of the thickness of the protein monolayer by ellipsometry show that the orientation of R-PE disk plane on the substrate is parallel to the plane of substrate. Absorption and fluorescence spectra of R-PE LB multilayers were obtained through transferring R-PE monolayer at the air-water interface to the substrates at the proper surface pressure by Langmuir-Blodgett (LB) technique. These spectra of R-PE LB films do not show distinct differences from those in aqueous solution. Comparative studies of circular dichroism (CD) spectra of the protein between in
文摘The antenna system of photosynthetic organisms serves to absorb light energy andtransfer excitation energy to the reaction centers. Energy transfer in the antenna system hasbeen found to be very efficient and rapid. The overall transfer efficiency exceeds 90％, andthe whole process of energy transfer from the phycoerythrin (PE) to the reaction center iscompleted within 50 ps in intact cells of red algae and cyanobacteria. Phycobilisome. the important photosynthetic antenna in red algae and cyanobacteria,consists of antenna polypeptide rods and core. One side of the core attaches to thethylakoid membrane and connects with the reaction center. the other side connects with
基金Project supported by the National Natural Science Foundation of China
文摘Through an electrochemical cell deposited with R-phycoerythrin (R-PE) monolayer on SnO2 optically transparent electrode (SnO2 OTE), charge transport phenomenon and the photoelectrochemical behavior of R-PE have been investigated. The experimental results indicate that the cell is able to generate photocurrent; moreover, the signal increases apparently in the presence of electron donor or acceptor in the electrolyte solution, showing that the photocurrent of R-PE would originate from its charge transfer. Further comparative test showed that the photocurrent came from the photo-induced charge separation property of the chromorphores attached covalently to the apoprotein of R-PE. The photocurrent spectrum of R-PE LB films verified the above viewpoint, from which the mechanism of photo-induced charge transfer of R-PE is suggested. The quantum yield for photoelectric conversion of R-PE LB films was measured to be φ520nm=3.4% and the photovoltage approached 400 mV. Moreover, the protein is stable for a
文摘Polysiphonia urceolata R phycoerythrin and Porphyridium cruentum B phycoerythrin were degraded with proteinaseK, and then the nearly native γ subunits were isolated from the reaction mixture. The process of degradation of phycoerythrin with proteinaseK showed that the γ subunit is located in the central cavity of (αβ) 6 hexamer of phycoerythrin. Comparative analysis of the spectra of the native phycoerythrin, the phycoerythrin at pH 12 and the isolated γ subunit showed that the absorption peaks of phycoerythrobilins on α or β subunit are at 535 nm (or 545 nm) and 565 nm, the fluorescence emission maximum at 580 nm; the absorption peak of phycoerythrobilins on the isolated γ subunit is at 589 nm, the fluorescence emission peak at 620 nm which overlaps the absorption maximum of C phycocyanin and perhaps contributes to the energy transfer with high efficiency between phycoerythrin and phycocyanin in phycobilisome; the absorption maximum of phycourobilin on the isolated γ subunit is at 498 nm, which is the same as that in native phycoerythrin, and the fluorescence emission maximum at 575 nm.
