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1.
Biofizika ; 55(2): 252-8, 2010.
Artigo em Russo | MEDLINE | ID: mdl-20429278

RESUMO

The joint effects of 0.5 M NaCI and light of different intensities on the activity of the photosynthetic apparatus and ATP contents in cells of the katG- mutant of cyanobacterium Synechocystis sp. PCC 6803 have been studied. The mutant demonstrated a higher photoinhibition rate and a slower rate of recovery compared to the wild type, as it was shown by measurements of the CO2-dependent O2 production and delayed light emission of Chl a. The presence of 0.5 M NaCl in incubation medium induced the equal photoinhibition of the photosynthetic apparatus at I = 1200 microE m(-2) x (-1) in the mutant and wild-type cells. At I = 2400 microE m(-2) x c(-1), a stronger inhibition and a slower recovery of the photosynthetic apparatus activity in the kat- mutant than in wild-type cells was observed. The data obtained evidence an important role of catalase-peroxidase in the system of reparation of the photosynthetic apparatus damaged by high-intensty light, especially against the background of NaCI stress.


Assuntos
Catalase/metabolismo , Fotossíntese/efeitos dos fármacos , Cloreto de Sódio/farmacologia , Synechocystis/enzimologia , Catalase/genética , Mutação , Synechocystis/genética , Synechocystis/crescimento & desenvolvimento
2.
Biokhimiia ; 48(10): 1604-10, 1983 Oct.
Artigo em Russo | MEDLINE | ID: mdl-6357291

RESUMO

It was demonstrated that the decrease of the activity of photosystem II in agranal chloroplasts of bundle sheath cells of malate C4 plants is due to a loss of the chlorophyll-protein complex of this photosystem. This is paralleled with an increase in the relative amount of the chlorophyll--protein complex of photosystem I and a partial loss of the light-harvesting pigmentprotein complex. These two events may account for the high activity of photosystem I and for the low content of chlorophyll b in the plastids. The cumulative data are indicative of a close interrelationship between the granal state of the chloroplast membranes and the presence of the chlorophyll--protein complex of photosystem II.


Assuntos
Clorofila/isolamento & purificação , Clorófitas/metabolismo , Proteínas de Plantas/isolamento & purificação , Plantas/metabolismo , Clorofila/metabolismo , Complexos de Proteínas Captadores de Luz , Fotossíntese , Complexo de Proteínas do Centro de Reação Fotossintética , Complexo de Proteína do Fotossistema I , Complexo de Proteína do Fotossistema II , Proteínas de Plantas/metabolismo , Especificidade da Espécie
3.
Biokhimiia ; 48(9): 1421-8, 1983 Sep.
Artigo em Russo | MEDLINE | ID: mdl-6354277

RESUMO

Three types of mutants (pigment, non-photosynthesizing and pigment non-photosynthesizing ones) were used to identify the chlorophyll-containing bands in gel slices. The pigment mutants with an impaired light-harvesting chlorophyll a/b-protein complex possess photochemically active reaction centers of photosystems and are capable of phototrophic growth. Using these mutants, the heterogeneity of the chlorophyll-containing bands, LH2 and LH3, in gel slices and the dependence of LH2 on chlorophyll a-protein and that of LH3 on chlorophyll b-protein in the light-harvesting complex were established. The non-photosynthesizing mutants with an inactive photosystem I (or II) are devoid of antennae forms of chlorophyll a and are not capable of phototrophic growth. Using these mutants, it was demonstrated that in gel slices the chlorophyll-containing band, CPI, corresponds to the chlorophyll a-protein complex of photosystem I, while CPII to the chlorophyll a-protein complex of photosystem II. It was also found that the presence of the chlorophyll-containing band, LH0 (CPIa) in gel slices correlates with the preservation of the light-harvesting complex and is independent of photosystem I. The spectral properties of chlorophyll complexes in gel slices are not identical to those of native chlorophyll. It was assumed that chloroplasts contain at least 4 types of chlorophyll proteins that are controlled by independent genes.


Assuntos
Chlamydomonas/metabolismo , Clorofila/isolamento & purificação , Mutação , Proteínas de Plantas/isolamento & purificação , Chlamydomonas/genética , Clorofila/metabolismo , Eletroforese/métodos , Luz , Complexos de Proteínas Captadores de Luz , Complexo de Proteínas do Centro de Reação Fotossintética , Complexo de Proteína do Fotossistema I , Complexo de Proteína do Fotossistema II , Proteínas de Plantas/metabolismo
4.
Biofizika ; 27(1): 37-41, 1982.
Artigo em Russo | MEDLINE | ID: mdl-7066400

RESUMO

Low temperature fluorescence spectra and second derivatives of chlorophyll absorption spectra in leaves, chloroplasts of mesophyll and parenchyme bundle sheath cells (BSC) were studied. It has been shown that in ontogenesis of BSC chloroplasts of Zea mays leaves along with a decrease of the activity of the PS-2 and a reduction of granal regions the fluorescence maximum of chlorophyll decreases at 695 nm. The change of this fluorescence band is concerned with the disturbance of the form of chlorophyll "a" absorbing at 684 nm and performing the function of an antenna of the pigment-protein complex of PS-2. Similarities in the distribution of chlorophyll forms between three pigment-protein complexes of chloroplast membranes in green algae and higher plants are discussed.


Assuntos
Clorofila/metabolismo , Cloroplastos/metabolismo , Fotossíntese , Clorófitas/metabolismo , Plantas/metabolismo , Espectrometria de Fluorescência , Zea mays/metabolismo
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