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1.
Nanotechnology ; 29(2): 025702, 2018 01 12.
Article in English | MEDLINE | ID: mdl-29130898

ABSTRACT

Nanostructures as color-tunable luminescent markers have become major, promising tools for bioimaging and biosensing. In this paper separated molybdate/Gd2O3 doped rare earth ions (erbium, Er3+ and ytterbium, Yb3+) core-shell nanoparticles (NPs), were fabricated by a one-step homogeneous precipitation process. Emission properties were studied by cathodo- and photoluminescence. Scanning electron and transmission electron microscopes were used to visualize and determine the size and shape of the NPs. Spherical NPs were obtained. Their core-shell structures were confirmed by x-ray diffraction and energy-dispersive x-ray spectroscopy measurements. We postulated that the molybdate rich core is formed due to high segregation coefficient of the Mo ion during the precipitation. The calcination process resulted in crystallization of δ/ξ (core/shell) NP doped Er and Yb ions, where δ-gadolinium molybdates and ξ-molybdates or gadolinium oxide. We confirmed two different upconversion mechanisms. In the presence of molybdenum ions, in the core of the NPs, Yb3+-[Formula: see text] (∣2F7/2, 3T2〉) dimers were formed. As a result of a two 980 nm photon absorption by the dimer, we observed enhanced green luminescence in the upconversion process. However, for the shell formed by the Gd2O3:Er, Yb NPs (without the Mo ions), the typical energy transfer upconversion takes place, which results in red luminescence. We demonstrated that the NPs were transported into cytosol of the HeLa and astrocytes cells by endocytosis. The core-shell NPs are sensitive sensors for the environment prevailing inside (shorter luminescence decay) and outside (longer luminescence decay) of the tested cells. The toxicity of the NPs was examined using MTT assay.


Subject(s)
Erbium/chemistry , Gadolinium/chemistry , Luminescent Agents/chemistry , Molybdenum/chemistry , Nanoparticles/chemistry , Optical Imaging/methods , Ytterbium/chemistry , Astrocytes/cytology , HeLa Cells , Humans , Luminescent Measurements/methods , Microscopy, Confocal/methods , Nanoparticles/ultrastructure , Nanotechnology/methods
2.
Plant Cell Physiol ; 57(7): 1495-1509, 2016 Jul.
Article in English | MEDLINE | ID: mdl-27273581

ABSTRACT

Natural capacity has evolved in higher plants to absorb and harness excessive light energy. In basic models, the majority of absorbed photon energy is radiated back as fluorescence and heat. For years the proton sensor protein PsbS was considered to play a critical role in non-photochemical quenching (NPQ) of light absorbed by PSII antennae and in its dissipation as heat. However, the significance of PsbS in regulating heat emission from a whole leaf has never been verified before by direct measurement of foliar temperature under changing light intensity. To test its validity, we here investigated the foliar temperature changes on increasing and decreasing light intensity conditions (foliar temperature dynamics) using a high resolution thermal camera and a powerful adjustable light-emitting diode (LED) light source. First, we showed that light-dependent foliar temperature dynamics is correlated with Chl content in leaves of various plant species. Secondly, we compared the foliar temperature dynamics in Arabidopsis thaliana wild type, the PsbS null mutant npq4-1 and a PsbS-overexpressing transgenic line under different transpiration conditions with or without a photosynthesis inhibitor. We found no direct correlations between the NPQ level and the foliar temperature dynamics. Rather, differences in foliar temperature dynamics are primarily affected by stomatal aperture, and rapid foliar temperature increase during irradiation depends on the water status of the leaf. We conclude that PsbS is not directly involved in regulation of foliar temperature dynamics during excessive light energy episodes.


Subject(s)
Plant Proteins/metabolism , Plant Stomata/physiology , Plants/metabolism , Temperature , Diuron/pharmacology , Light , Linear Models , Models, Biological , Organ Specificity/drug effects , Organ Specificity/radiation effects , Photosynthesis/drug effects , Photosynthesis/radiation effects , Plant Stomata/drug effects , Plant Stomata/radiation effects , Plant Transpiration/drug effects , Plant Transpiration/radiation effects , Plants/drug effects , Plants/radiation effects
3.
Plant Signal Behav ; 10(1): e982018, 2015.
Article in English | MEDLINE | ID: mdl-25654166

ABSTRACT

Systemic acquired acclimation (SAA) is an important light acclimatory mechanism that depends on the global adjustments of non-photochemical quenching and chloroplast retrograde signaling. As the exact regulation of these processes is not known, we measured time-resolved fluorescence of chlorophyll a in Arabidopsis thaliana leaves exposed to excess light, in leaves undergoing SAA, and in leaves after excess light episode. We compare the behavior induced in wild-type plants with null mutant of non-photochemical quenching (npq4-1). The wild type rosettes exhibit a small reduction of fluorescence decay times in leaves directly exposed to excess light and in leaves undergoing SAA in ambient low light. However in npq4-1 exposition to excess light results in much faster fluorescence decay, which is insensitive to excitation power. At the same time npq4-1 leaves undergoing SAA displayed intermediate fluorescence decay. The npq4-1 plants also lost the ability to optimize florescence decay, and thus chlorophyll a dynamics up to 2 h after excess light episode. The fluorescence decay dynamics in both WT and npq4-1 can be described by a set of 3 maximum decay times. Based on the results, we concluded that functional PsbS is required for optimization of absorbed photon fate and optimal light acclimatory responses such as SAA or after excess light stress.


Subject(s)
Acclimatization/physiology , Arabidopsis Proteins/metabolism , Arabidopsis/physiology , Chlorophyll/physiology , Light-Harvesting Protein Complexes/metabolism , Light , Photosystem II Protein Complex/metabolism , Stress, Physiological/radiation effects , Arabidopsis/genetics , Arabidopsis Proteins/genetics , Fluorescence , Light-Harvesting Protein Complexes/genetics , Mutation , Photosystem II Protein Complex/genetics , Time Factors
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