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1.
Photosynth Res ; 111(1-2): 193-204, 2012 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-21833799

RESUMO

Chlorosomes, the light-harvesting antennae of green photosynthetic bacteria, are based on large aggregates of bacteriochlorophyll molecules. Aggregates with similar properties to those in chlorosomes can also be prepared in vitro. Several agents were shown to induce aggregation of bacteriochlorophyll c in aqueous environments, including certain lipids, carotenes, and quinones. A key distinguishing feature of bacteriochlorophyll c aggregates, both in vitro and in chlorosomes, is a large (>60 nm) red shift of their Q(y) absorption band compared with that of the monomers. In this study, we investigate the self-assembly of bacteriochlorophyll c with the xanthophyll astaxanthin, which leads to the formation of a new type of complexes. Our results indicate that, due to its specific structure, astaxanthin molecules competes with bacteriochlorophylls for the bonds involved in the aggregation, thus preventing the formation of any significant red shift compared with pure bacteriochlorophyll c in aqueous buffer. A strong interaction between both the types of pigments in the developed assemblies, is manifested by a rather efficient (~40%) excitation energy transfer from astaxanthin to bacteriochlorophyll c, as revealed by fluorescence excitation spectroscopy. Results of transient absorption spectroscopy show that the energy transfer is very fast (<500 fs) and proceeds through the S(2) state of astaxanthin.


Assuntos
Proteínas de Bactérias/química , Bacterioclorofilas/química , Chlorobium/química , Transferência de Energia , Complexos de Proteínas Captadores de Luz/química , Proteínas de Bactérias/isolamento & purificação , Proteínas de Bactérias/metabolismo , Bacterioclorofilas/isolamento & purificação , Bacterioclorofilas/metabolismo , Luz , Complexos de Proteínas Captadores de Luz/metabolismo , Fotossíntese , Análise Espectral , Xantofilas/química
2.
Food Chem ; 129(3): 1054-9, 2011 Dec 01.
Artigo em Inglês | MEDLINE | ID: mdl-25212336

RESUMO

Sensory attributes, texture and fatty acid profiles of fillets of Eurasian perch (Percafluviatilis L.) reared under two conditions were compared. Perch were reared either in an extensive pond-based (EC) system in polyculture with carp, or intensively cultured (IC) in a recirculation system. Attributes of raw and cooked fillets of marketable perch (120-150g) were compared. No significant differences were found between groups for odour, flavour, aftertaste, or consistency in subjective evaluation of cooked fillets. The texture profile analysis (TPA) showed raw fillets from the EC group to exhibit higher values of hardness, springiness, cohesiveness, and gumminess than the IC group. Fish from the IC group had a lower content of saturated fatty acids (SFA) and polyunsaturated fatty acids (PUFA) and a higher content of monounsaturated fatty acids (MUFA) in comparison to EC perch. The proportion of iso- and anteiso-SFAs was 2.6% in the EC group and 0.75% in the IC group. The content of n-3 PUFA was lower in IC than in EC, while the content of n-6 PUFA was higher in IC than in EC. The ratio of n-3:n-6 PUFA was 1.42 for the IC group and 2.85 for the EC group.

3.
Micron ; 38(2): 170-5, 2007.
Artigo em Inglês | MEDLINE | ID: mdl-16962333

RESUMO

Oxygenic photosynthesis of higher plants requires linear electron transport that is driven by serially operating Photosystem II and Photosystem I reaction centers. It is widely accepted that distribution of these two types of reaction centers in the thylakoid membrane is heterogeneous. Here, we describe two optical microscopic techniques that can be combined to reveal the heterogeneity. By imaging micro-spectroscopy at liquid nitrogen temperature, we resolved the heterogeneity of the chloroplast thylakoid membrane by distinct spectral signatures of fluorescence emitted by the two photosystems. With another microscope, we measured changes in the fluorescence emission yield that are induced by actinic light at room temperature. Fluorescence yield of Photosystem II reaction centers varies strongly with light-induced changes of its photochemical yield. Consequently, application of moderate background irradiance induces changes in the Photosystem II fluorescence yield whereas no such modulation occurs in Photosystem I. This contrasting feature was used to identify regions in thylakoid membranes that are enriched in active Photosystem II.


Assuntos
Microscopia de Fluorescência/métodos , Complexo de Proteína do Fotossistema I/análise , Complexo de Proteína do Fotossistema II/análise , Espectrometria de Fluorescência/métodos , Tilacoides/química , Processamento de Imagem Assistida por Computador , Microscopia Eletrônica de Transmissão , Tilacoides/ultraestrutura
4.
Photosynth Res ; 68(3): 203-13, 2001.
Artigo em Inglês | MEDLINE | ID: mdl-16228343

RESUMO

Tobacco plants (Nicotiana tabacum) were kept in CO(2) free air for several days to investigate the effect of lack of electron acceptors on the photosynthetic electron transport chain. CO(2) starvation resulted in a dramatic decrease in photosynthetic activity. Measurements of the electron transport activity in thylakoid membranes showed that a loss of Photosystem II activity was mainly responsible for the observed decrease in photosynthetic activity. In the absence of CO(2) the plastoquinone pool and the acceptor side of Photosystem I were highly reduced in the dark as shown by far-red light effects on chlorophyll fluorescence and P700 absorption measurements. Reduction of the oxygen content of the CO(2) free air retarded photoinhibitory loss of photosynthetic activity and pigment degradation. Electron flow to oxygen seemed not to be able to counteract the stress induced by severe CO(2) starvation. The data are discussed in terms of a donation of reducing equivalents from mitochondria to chloroplasts and a reduction of the plastoquinone pool via the NAD(P)H-plastoquinone oxidoreductase during CO(2) starvation.

5.
J Photochem Photobiol B ; 59(1-3): 103-14, 2000 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-11332877

RESUMO

The spectral characteristics of chlorophyll fluorescence and absorption during linear heating of barley leaves within the range 25-75 degreesC (fluorescence temperature curve, FTC) were studied. Leaves with various content of light harvesting complexes (green, Chl b-less chlorina f2 and intermittent light grown) revealing different types of FTC were used. Differential absorption, emission and excitation spectra documented four characteristic phases of the FTC. The initial two FTC phases (a rise in the 46-49 degreesC region and a subsequent decrease to about 55 degreesC) mostly reflected changes in the fluorescence quantum yield peaking at about 685 nm. A steep second fluorescence rise at 55-61 degreesC was found to originate from a short-wavelength Chl a spectral form (emission maximum at 675 nm) causing a gradual blue shift of the emission spectra. In this temperature range, a clear correspondence of the blue shift in the emission and absorption spectra was found. We suggest that the second fluorescence rise in FTC reflects a weakening of the Chl a-protein interaction in the thylakoid membrane.


Assuntos
Clorofila/metabolismo , Calefação , Hordeum/metabolismo , Complexo de Proteínas do Centro de Reação Fotossintética/metabolismo , Clorofila A , Fluorescência , Complexos de Proteínas Captadores de Luz , Folhas de Planta/metabolismo , Espectrometria de Fluorescência/métodos
6.
Proc Natl Acad Sci U S A ; 92(7): 2929-33, 1995 Mar 28.
Artigo em Inglês | MEDLINE | ID: mdl-11607522

RESUMO

A reaction center of photosystem II was isolated from Pisum sativum by using immobilized metal affinity chromatography. This reaction center is photochemically active and has a room temperature Qgamma chlorophyll (Chl) absorption band peaking at 677.5 nm. From HPLC analysis, the pigment stoichiometry was suggested to be 5 Chls per 1 beta-carotene per 2 pheophytins. Low-temperature absorption measurements at 77 K were consistent with the removal of one of the Chls associated with the usual form of the reaction center isolated by using ion-exchange chromatography. Transient absorption spectroscopy on the picosecond time scale indicated that the Chl removed belongs to a pool of Chl absorbing at approximately 670 nm (C670II) that transfers energy relatively slowly to the primary donor P680 in support of our recently proposed model. The results also support the previous conclusion that radical pair formation is largely associated with a 21-ps time constant when P680 is directly excited and that the identity of C670II is likely to be peripherally bound Chls possibly ligated to conserved His residues at positions 118 on the D1 and D2 proteins.

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