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1.
Biochim Biophys Acta ; 1847(4-5): 486-492, 2015.
Artigo em Inglês | MEDLINE | ID: mdl-25615585

RESUMO

When cyanobacteria are grown under iron-limited or other oxidative stress conditions the iron stress inducible pigment-protein IsiA is synthesized in variable amounts. IsiA accumulates in aggregates inside the photosynthetic membrane that strongly dissipate chlorophyll excited state energy. In this paper we applied Stark fluorescence (SF) spectroscopy at 77K to IsiA aggregates to gain insight into the nature of the emitting and energy dissipating state(s). Our study shows that two emitting states are present in the system, one emitting at 684 nm and the other emitting at about 730 nm. The new 730 nm state exhibits strongly reduced fluorescence (F) together with a large charge transfer character. We discuss these findings in the light of the energy dissipation mechanisms involved in the regulation of photosynthesis in plants, cyanobacteria and diatoms. Our results suggest that photosynthetic organisms have adopted common mechanisms to cope with the deleterious effects of excess light under unfavorable growth conditions.


Assuntos
Proteínas de Bactérias/metabolismo , Clorofila/metabolismo , Cianobactérias/metabolismo , Complexos de Proteínas Captadores de Luz/metabolismo , Fotossíntese/fisiologia , Complexo de Proteína do Fotossistema I/metabolismo , Proteínas de Bactérias/química , Cianobactérias/crescimento & desenvolvimento , Fluorescência , Complexos de Proteínas Captadores de Luz/química , Complexo de Proteína do Fotossistema I/química , Espectrometria de Fluorescência , Estresse Fisiológico
2.
Biophys J ; 84(1): 440-9, 2003 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-12524297

RESUMO

We have measured low-intensity, polarized one-color pump-probe traces in the B800 band of the light-harvesting complex LH2 of Rhodospirillum molischianum at 77 K. The excitation/detection wavelength was tuned through the B800 band. A single-wavelength and a global target analysis of the data were performed with a model that accounts for excitation energy transfer among the B800 molecules and from B800 to B850. By including the anisotropy of the signals into the fitting procedure, both transfer processes could be separated. It was estimated in the global target analysis that the intra-B800 energy transfer, i.e., the hopping of the excitation from one B800 to another B800 molecule, takes approximately 0.5 ps at 77 K. This transfer time increases with the excitation/detection wavelength from 0.3 ps on the blue side of the B800 band to approximately 0.8 ps on the red side. The residual B800 anisotropy shows a wavelength dependence as expected for energy transfer within an inhomogeneously broadened cluster of weakly coupled pigments. In the global target analysis, the transfer time from B800 to B850 was determined to be approximately 1.7 ps at 77 K. In the single-wavelength analysis, a speeding-up of the B800 --> B850 energy transfer rate toward the blue edge of the B800 band was found. This nicely correlates with the proposed position of the suggested high-exciton component of the B850 band acting as an additional decay channel for B800 excitations.


Assuntos
Proteínas de Bactérias/química , Proteínas de Bactérias/efeitos da radiação , Complexo de Proteínas do Centro de Reação Fotossintética/química , Protoclorifilida/química , Protoclorifilida/efeitos da radiação , Rhodospirillum/química , Rhodospirillum/efeitos da radiação , Anisotropia , Proteínas de Bactérias/metabolismo , Células Cultivadas , Relação Dose-Resposta à Radiação , Transferência de Energia , Lasers , Luz , Modelos Biológicos , Estimulação Luminosa , Complexo de Proteínas do Centro de Reação Fotossintética/metabolismo , Complexo de Proteínas do Centro de Reação Fotossintética/efeitos da radiação , Protoclorifilida/metabolismo , Rhodospirillum/metabolismo , Sensibilidade e Especificidade
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