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1.
Eur Biophys J ; 37(6): 843-50, 2008 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-18286272

RESUMO

Singlet oxygen (1O2) generation in the reaction centers (RCs) of Rhodobacter sphaeroides wild type was characterized by luminescent emission in the near infrared region (time resolved transients and emission spectra) and quantified to have quantum yield of 0.03 +/- 0.005. 1O2 emission was measured as a function of temperature, ascorbate, urea and potassium ferricyanide concentrations and as a function of incubation time in H2O:D2O mixtures. 1O2 was shown to be affected by the RC dynamics and to originate from the reaction of molecular oxygen with two sources of triplets: photoactive dimer formed by singlet-triplet mixing and bacteriopheophytin formed by direct photoexcitation and intersystem crossing.


Assuntos
Modelos Biológicos , Complexo de Proteínas do Centro de Reação Fotossintética/química , Complexo de Proteínas do Centro de Reação Fotossintética/metabolismo , Rhodobacter sphaeroides/química , Rhodobacter sphaeroides/fisiologia , Oxigênio Singlete/química , Oxigênio Singlete/metabolismo , Simulação por Computador , Complexo de Proteínas do Centro de Reação Fotossintética/efeitos da radiação , Rhodobacter sphaeroides/efeitos da radiação
2.
J Plant Physiol ; 160(6): 657-66, 2003 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-12872488

RESUMO

Three high-yielding wheat genotypes (T. aestivum L., c.v. Siete Cerros, Seri and Bacanora, released in 1966, 1982 and 1988, respectively) were grown under irrigation in two high radiation, low relative humidity environments (Tlaltizapan and Ciudad Obregon CIMMYT experimental stations, Mexico). Gas exchange and fluorescence parameters were assessed on the flag leaf during the day. Carbon isotope discrimination (delta) was analysed in flag leaf at anthesis and in grain at maturity. In both environments, gas exchange and fluorescence parameters varied markedly with irradiance and temperature. Analysis of their respective variation indicated the occurrence of photo-respiration and photo-inhibition, particularly in Tlaltizapan, the warmest environment, and in Siete Cerros. In Ciudad Obregon (high-yielding environment) lower Ci (internal CO2 concentration) and delta La (carbon isotope discrimination of the leaf) suggested a higher intrinsic photosynthetic capacity in the variety Bacanora. Higher yield of this genotype was also associated with higher Fv'/Fo' (ratio of photochemical and non photochemical rate constants in the light) and Fm'/Fm (ratio of the non photochemical rate constants in the dark and light adapted state).


Assuntos
Aclimatação/fisiologia , Fotossíntese/fisiologia , Triticum/fisiologia , Aclimatação/efeitos da radiação , Dióxido de Carbono/metabolismo , Isótopos de Carbono/metabolismo , Respiração Celular/fisiologia , Respiração Celular/efeitos da radiação , Variação Genética , Genótipo , Temperatura Alta , Luz , Fotossíntese/efeitos da radiação , Complexo de Proteínas do Centro de Reação Fotossintética/metabolismo , Complexo de Proteínas do Centro de Reação Fotossintética/efeitos da radiação , Folhas de Planta/fisiologia , Folhas de Planta/efeitos da radiação , Sementes/fisiologia , Sementes/efeitos da radiação , Triticum/genética , Triticum/efeitos da radiação
3.
Plant Physiol ; 129(3): 1127-37, 2002 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-12114567

RESUMO

Phytochrome (phy) A mediates two distinct photobiological responses in plants: the very-low-fluence response (VLFR), which can be saturated by short pulses of very-low-fluence light, and the high-irradiance response (HIR), which requires prolonged irradiation with higher fluences of far-red light (FR). To investigate whether the VLFR and HIR involve different domains within the phyA molecule, transgenic tobacco (Nicotiana tabacum cv Xanthi) and Arabidopsis seedlings expressing full-length (FL) and various deletion mutants of oat (Avena sativa) phyA were examined for their light sensitivity. Although most mutants were either partially active or inactive, a strong differential effect was observed for the Delta6-12 phyA mutant missing the serine-rich domain between amino acids 6 and 12. Delta6-12 phyA was as active as FL phyA for the VLFR of hypocotyl growth and cotyledon unfolding in Arabidopsis, and was hyperactive in the VLFR of hypocotyl growth and cotyledon unfolding in tobacco, and the VLFR blocking subsequent greening under white light in Arabidopsis. In contrast, Delta6-12 phyA showed a dominant-negative suppression of HIR in both species. In hypocotyl cells of Arabidopsis irradiated with FR phyA:green fluorescent protein (GFP) and Delta6-12 phyA:GFP fusions localized to the nucleus and coalesced into foci. The proportion of nuclei with abundant foci was enhanced by continuous compared with hourly FR provided at equal total fluence in FL phyA:GFP, and by Delta6-12 phyA mutation under hourly FR. We propose that the N-terminal serine-rich domain of phyA is involved in channeling downstream signaling via the VLFR or HIR pathways in different cellular contexts.


Assuntos
Avena/fisiologia , Núcleo Celular/metabolismo , Fitocromo/metabolismo , Serina/metabolismo , Antocianinas/metabolismo , Arabidopsis/genética , Arabidopsis/fisiologia , Proteínas de Arabidopsis , Avena/genética , Avena/efeitos da radiação , Proteínas de Fluorescência Verde , Hipocótilo/crescimento & desenvolvimento , Luz , Proteínas Luminescentes/genética , Proteínas Luminescentes/metabolismo , Microscopia de Fluorescência , Mutação , Fotossíntese/fisiologia , Fotossíntese/efeitos da radiação , Complexo de Proteínas do Centro de Reação Fotossintética/metabolismo , Complexo de Proteínas do Centro de Reação Fotossintética/efeitos da radiação , Fitocromo/química , Fitocromo/genética , Fitocromo A , Plantas Geneticamente Modificadas , Proteínas Recombinantes de Fusão/genética , Proteínas Recombinantes de Fusão/metabolismo , Sementes/genética , Sementes/fisiologia , Sementes/efeitos da radiação , Transdução de Sinais/fisiologia , Nicotiana/genética , Nicotiana/fisiologia
4.
Biophys J ; 63(6): 1613-22, 1992 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-1489915

RESUMO

The effects of hydrostatic pressure on the excited state reactions of the photosynthetic system of cyanobacteria were studied with the use of stationary and dynamic fluorescence spectroscopy. When the cells were excited with blue light (442 nm), hydrostatic pressure promoted a large increase in the fluorescence emission of the phycobilisomes (PBS). When PBS were excited at 565 nm, the shoulder originating from photosystem II (PSII) emission (F685) disappeared under 2.4 kbar compression, suggesting suppression of the energy transfer from PBS to PSII. At atmospheric pressure, the excited state decay was complex due to energy transfer processes, and the best fit to the data consisted of a broad Lorentzian distribution of short lifetimes. At 2.4 kbar, the decay data changed to a narrower distribution of longer lifetimes, confirming the pressure-induced suppression of the energy transfer between the PBS and PSII. When the cells were excited with blue light, the decay at atmospheric pressure was even more complex and the best fit to the data consisted of a two-component Lorentzian distribution of short lifetimes. Under compression, the broad distribution of lifetimes spanning the region 100-1,000 ps disappeared and gave rise to the appearance of a narrow distribution characteristic of the PBS centered at 1.2 ns. The emission of photosystem I underwent 2.2-fold increase at 2.4 kbar and room temperature. A decrease in temperature from 20 to -10 degrees C at 2.4 kbar promoted a further increase in the fluorescence emission from photosystem I to a level comparable with that obtained at temperatures below 120 degrees K and atmospheric pressure. On the other hand, when the temperature was decreased under pressure, the PBS emission diminished to very low value at blue or green excitation, suggesting the disassembly into the phycobiliprotein subunits.


Assuntos
Cianobactérias/química , Fotossíntese , Fenômenos Biofísicos , Biofísica , Temperatura Baixa , Cianobactérias/efeitos da radiação , Transferência de Energia/efeitos da radiação , Pressão Hidrostática , Luz , Fotossíntese/efeitos da radiação , Complexo de Proteínas do Centro de Reação Fotossintética/química , Complexo de Proteínas do Centro de Reação Fotossintética/efeitos da radiação , Complexo de Proteína do Fotossistema I , Complexo de Proteína do Fotossistema II , Ficobilissomas , Espectrometria de Fluorescência
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