Photosynthetic oxygen evolution from photosystem II particles was analyzed as consequence of a train of short (5 μs) flashes of different light quality and different intensities to study cyclic electron flow around photosystem II. Damped oscillations of the amplitudes of O2-evolution corresponding to a flash sequence were fitted numerically and analyzed in terms of a nonhomogeneous distribution of misses, represented by the probability parameter αi. Application of red light, known to promote cyclic electron flow around photosystem II (Gruszecki et al., 1995) results in a considerable increase of all αi, indicating that at the molecular level the misses may be interpreted as resulting from a competition for the reduction of oxidized P680 between cyclic electron flow and the electron flow coming from the water splitting enzyme. In accordance with previous findings, application of light flashes of the spectrum covering the absorption region of carotenoids resulted in an inhibition of cyclic electron flow and a pronounced decrease of the level of the miss parameter. Possible molecular mechanisms for the activity control of this cyclic electron transport around photosystem II by carotenoids are discussed.
In pancreatic acinar cells stimulation of different intracellular pathways leads to different patterns of Ca2+ signaling. Bombesin induces activation of both phosphatidylinositol 4,5-bisphosphate (PIP2)-specific phospholipase C (PLC) and phospholipase D (PLD). The latter leads to generation of diacylglycerol (DAG) in addition to that produced by activation of PIP2-PLC. Strong activation of protein kinase C (PKC) results in inhibition of Ca2+-induced Ca2+ release from Ca2+ pools arranged in sequence to the luminally located IP3-sensitive Ca2+ pools. Consequently the Ca2+ wave which starts in the luminal cell pole is slower in the presence of bombesin (5 μm/s) as compared to that in the presence of acetylcholine (17 μm/s) which activates PIP2-PLC but not PLD. Activation of high-affinity CCK-receptors triggers a Ca2+ wave with slow propagation (5 μm/s) due to stimulation of phospholipase A2 (PLA2) and generation of arachidonic acid, which in turn leads to inhibition of Ca2+-induced Ca2+ release. Low-affinity CCK-receptors are coupled to both PIP2-PLC and PLD.
In our previous study (Gruszecki et al., 1995) we have postulated that the mechanism of cyclic electron transport around photosystem II, active under overexcitation of the photosynthetic apparatus by light is under control of the xanthophyll cycle. The combination of different light quality and thylakoids having various levels of xanthophyll cycle pigments were applied to support this hypothesis. In the present work photosynthetic oxygen evolution from isolated tobacco chloroplasts was measured by means of mass spectrometry under conditions of high or low levels of violaxanthin, being transformed to zeaxanthin during dark incubation in an ascorbate containing buffer at pH 5.7. Analysis of oxygen evolution and of light-induced oxygen uptake indicate that the de-epoxidation of violaxanthin to zeaxanthin results in an increased cyclic electron transport around PS II, thus dimishing the vectorial electron flow from water. An effect similar to de-epoxidation was observed after incubation of thylakoid membranes with specific antibodies against violaxanthin.
Light-driven electron transport in liposome-bound photosystem II (PS-II) particles between water and ferricyanide was monitored by bare platinum electrode oxymetry. The modification of the experimental system with the exogenous quinones α-tocopherol quinone ( α-TQ) or plastoquinone (PQ) resulted in a pronounced effect on photosynthetic oxygen evolution. The presence of α-tocopherolquinone ( α-TQ) in PS-II samples decreased the rate of red light-induced oxygen evolution but increased the rate of green light-induced oxygen evolution. Blue light applied to the assay system in which oxygen evolution was saturated by red light resulted in a further increase of the oxygen signal. These findings are interpreted in terms of a cyclic electron transport around PS-II, regulated by an excitation state of β-carotene in the reaction centre of PS-II. A mechanism is postulated according to which energetic coupling of β-carotene in the reaction centre of PS-II and that of other antenna carotenoid pigments is regulated by the portion of the xanthophyll violaxanthin, which is under control of the xanthophyll cycle.
The structure of the xanthophyll pigments lutein and zeaxanthin differs in the position of one double bond and refers to one of the ionon rings. Specific antibodies to zeaxanthin were used to analyse the localisation and orientation of these two xanthophyll pigments in lipid membranes formed with egg yolk lecithin. Bimolecular and monomolecular layers were used. Antibody-antigen interaction was demonstrated and analysed by the bathochromic shift of the absorption spectra of both pigments and by the increase of light-scattering of the pig- mented liposome suspension. It appeared that the extent of the spectral effects accompanying the interaction of the antiserum to zeaxanthin, injected to the liposome suspension which was pigmented with either zeaxanthin or lutein, was different in spite of their similar molecular structures. The results are interpreted in terms of a localisation and distribution of lutein, in the hydrophobic phase of liposomes within two essentially different pigment pools, one oriented horizontally and the other vertically with respect to the membrane plane. This inter- pretation is supported by the analysis of isotherms of the compression of monomolecular layers of lutein and zeaxanthin formed at the air-water interface and of mixed xanthophyll- lipid monolayers as well as by analysis of the penetration of antibody proteins dissolved in the subphase into the mixed xanthophyll-lipid films.