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1.
Microsc Microanal ; 28(1): 218-226, 2022 02.
Artículo en Inglés | MEDLINE | ID: mdl-35177134

RESUMEN

Alga in the genus Chroothece have been reported mostly from aquatic or subaerial continental environments, where they grow in extreme conditions. The strain Chroothece mobilis MAESE 20.29 was exposed to different light intensities, red and green monochromatic light, ultraviolet (UV) radiation, high nitrogen concentrations, and high salinity to assess the effect of those environmental parameters on its growth. Confocal laser scanning microscopy (CLSM) was used as an "in vivo" noninvasive single-cell method for the study. The strain seemed to prefer fairly high light intensities and showed a significant increase in allophycocyanin (APC) and chlorophyll a [photosystem I (PSI) and photosystem II (PSII)] fluorescence with 330 and 789 µM/cm2/s intensities. Green monochromatic light promoted a significant increase in the fluorescence of APC and chlorophyll a (PSI and PSII). UV-A significantly decreased phycocyanin and increased APC, while UV-A + B showed a greater decreasing effect on c-Phycocyanin but did not significantly change concentrations of APC. The increase in nitrogen concentration in the culture medium significantly and negatively affected all pigments, and no effect was observed with an increase in salinity. Our data show that CLSM represents a very powerful tool for ecological research of microalgae in small volumes and may contribute to the knowledge of phycobiliproteins in vivo behavior and the parameters for the large-scale production of these pigments.


Asunto(s)
Complejo de Proteína del Fotosistema I , Rhodophyta , Clorofila , Clorofila A , Microscopía Confocal , Complejo de Proteína del Fotosistema I/metabolismo , Complejo de Proteína del Fotosistema I/efectos de la radiación , Complejo de Proteína del Fotosistema II/metabolismo , Complejo de Proteína del Fotosistema II/efectos de la radiación , Rhodophyta/metabolismo
2.
Int J Mol Sci ; 22(21)2021 Oct 26.
Artículo en Inglés | MEDLINE | ID: mdl-34768948

RESUMEN

The objective of our study was to characterise the growth of tomato seedlings under various light spectra, but special attention has been paid to gaining a deeper insight into the details of photosynthetic light reactions. The following light combinations (generated by LEDs, constant light intensity at 300 µmol m-2 s-1) were used: blue/red light; blue/red light + far red; blue/red light + UV; white light that was supplemented with green, and white light that was supplemented with blue. Moreover, two combinations of white light for which the light intensity was changed by imitating the sunrise, sunset, and moon were also tested. The reference point was also light generated by high pressure sodium lamps (HPS). Plant growth/morphological parameters under various light conditions were only partly correlated with the photosynthetic efficiency of PSI and PSII. Illumination with blue/red as the main components had a negative effect on the functioning of PSII compared to the white light and HPS-generated light. On the other hand, the functioning of PSI was especially negatively affected under the blue/red light that was supplemented with FR. The FT-Raman studies showed that the general metabolic profile of the leaves (especially proteins and ß-carotene) was similar in the plants that were grown under the HPS and under the LED-generated white light for which the light intensity changed during a day. The effect of various light conditions on the leaf hormonal balance (auxins, brassinosteroids) is also discussed.


Asunto(s)
Fotosíntesis , Solanum lycopersicum/metabolismo , Solanum lycopersicum/efectos de la radiación , Brasinoesteroides/metabolismo , Clorofila/metabolismo , Ácidos Indolacéticos/metabolismo , Luz , Solanum lycopersicum/crecimiento & desarrollo , Metaboloma , Fotosíntesis/efectos de la radiación , Complejo de Proteína del Fotosistema I/metabolismo , Complejo de Proteína del Fotosistema I/efectos de la radiación , Complejo de Proteína del Fotosistema II/metabolismo , Complejo de Proteína del Fotosistema II/efectos de la radiación , Reguladores del Crecimiento de las Plantas/metabolismo , Hojas de la Planta/crecimiento & desarrollo , Hojas de la Planta/metabolismo , Hojas de la Planta/efectos de la radiación , Plantones/crecimiento & desarrollo , Plantones/metabolismo , Plantones/efectos de la radiación , Espectrometría Raman
3.
ACS Appl Mater Interfaces ; 13(9): 11237-11246, 2021 Mar 10.
Artículo en Inglés | MEDLINE | ID: mdl-33621059

RESUMEN

Photobioelectrodes represent one of the examples where artificial materials are combined with biological entities to undertake semi-artificial photosynthesis. Here, an approach is described that uses reduced graphene oxide (rGO) as an electrode material. This classical 2D material is used to construct a three-dimensional structure by a template-based approach combined with a simple spin-coating process during preparation. Inspired by this novel material and photosystem I (PSI), a biophotovoltaic electrode is being designed and investigated. Both direct electron transfer to PSI and mediated electron transfer via cytochrome c from horse heart as redox protein can be confirmed. Electrode preparation and protein immobilization have been optimized. The performance can be upscaled by adjusting the thickness of the 3D electrode using different numbers of spin-coating steps during preparation. Thus, photocurrents up to ∼14 µA/cm2 are measured for 12 spin-coated layers of rGO corresponding to a turnover frequency of 30 e- PSI-1 s-1 and external quantum efficiency (EQE) of 0.07% at a thickness of about 15 µm. Operational stability has been analyzed for several days. Particularly, the performance at low illumination intensities is very promising (1.39 µA/cm2 at 0.1 mW/cm2 and -0.15 V vs Ag/AgCl; EQE 6.8%).


Asunto(s)
Proteínas Bacterianas/química , Electrodos , Grafito/química , Complejo de Proteína del Fotosistema I/química , Animales , Proteínas Bacterianas/efectos de la radiación , Citocromos c/química , Electricidad , Caballos , Proteínas Inmovilizadas/química , Luz , Complejo de Proteína del Fotosistema I/efectos de la radiación , Thermosynechococcus/enzimología
4.
Plant Cell Environ ; 44(9): 3002-3014, 2021 09.
Artículo en Inglés | MEDLINE | ID: mdl-33599977

RESUMEN

Vascular plants use carotenoids and chlorophylls a and b to harvest solar energy in the visible region (400-700 nm), but they make little use of the far-red (FR) light. Instead, some cyanobacteria have developed the ability to use FR light by redesigning their photosynthetic apparatus and synthesizing red-shifted chlorophylls. Implementing this strategy in plants is considered promising to increase crop yield. To prepare for this, a characterization of the FR light-induced changes in plants is necessary. Here, we explore the behaviour of Arabidopsis thaliana upon exposure to FR light by following the changes in morphology, physiology and composition of the photosynthetic complexes. We found that after FR-light treatment, the ratio between the photosystems and their antenna size drastically readjust in an attempt to rebalance the energy input to support electron transfer. Despite a large increase in PSBS accumulation, these adjustments result in strong photoinhibition when FR-adapted plants are exposed to light again. Crucially, FR light-induced changes in the photosynthetic membrane are not the result of senescence, but are a response to the excitation imbalance between the photosystems. This indicates that an increase in the FR absorption by the photosystems should be sufficient for boosting photosynthetic activity in FR light.


Asunto(s)
Adaptación Fisiológica/efectos de la radiación , Arabidopsis/efectos de la radiación , Luz , Arabidopsis/fisiología , Clorofila/metabolismo , Fluorescencia , Complejos de Proteína Captadores de Luz/efectos de la radiación , Fotosíntesis/efectos de la radiación , Complejo de Proteína del Fotosistema I/efectos de la radiación , Complejo de Proteína del Fotosistema II/efectos de la radiación , Hojas de la Planta/efectos de la radiación , Tilacoides/efectos de la radiación
5.
Plant Sci ; 303: 110795, 2021 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-33487367

RESUMEN

Under natural field conditions, plants usually experience fluctuating light (FL) under moderate heat stress in summer. However, responses of photosystems I and II (PSI and PSII) to such combined stresses are not well known. Furthermore, the role of water-water cycle (WWC) in photoprotection in FL under moderate heat stress is poorly understood. In this study, we examined chlorophyll fluorescence and P700 redox state in FL at 42 °C in two orchids, Dendrobium officinale (with high WWC activity) and Bletilla striata (with low WWC activity). After FL treatment at 42 °C, PSI activity maintained stable while PSII activity decreased significantly in these two orchids. In D. officinale, the WWC could rapidly consume the excess excitation energy in PSI and thus avoided an over-reduction of PSI upon any increase in illumination. Therefore, in D. officinale, WWC likely protected PSI in FL at 42 °C. In B. striata, heat-induced PSII photoinhibition down-regulated electron flow from PSII and thus prevented an over-reduction of PSI after transition from low to high light. Consequently, in B. striata moderate PSII photoinhibition could protected PSI in FL at 42 °C. We conclude that, in addition to cyclic electron flow, WWC and PSII photoinhibition-repair cycle are two important strategies for preventing PSI photoinhibition in FL under moderate heat stress.


Asunto(s)
Dendrobium/metabolismo , Orchidaceae/metabolismo , Complejo de Proteína del Fotosistema I/fisiología , Dendrobium/fisiología , Respuesta al Choque Térmico , Luz , Oxidación-Reducción , Complejo de Proteína del Fotosistema I/metabolismo , Complejo de Proteína del Fotosistema I/efectos de la radiación , Complejo de Proteína del Fotosistema II/metabolismo , Complejo de Proteína del Fotosistema II/fisiología , Complejo de Proteína del Fotosistema II/efectos de la radiación
6.
Photosynth Res ; 147(1): 91-106, 2021 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-33280077

RESUMEN

Most photosynthetic organisms are sensitive to very high light, although acclimation mechanisms enable them to deal with exposure to strong light up to a point. Here we show that cultures of wild-type Chlamydomonas reinhardtii strain cc124, when exposed to photosynthetic photon flux density 3000 µmol m-2 s-1 for a couple of days, are able to suddenly attain the ability to grow and thrive. We compared the phenotypes of control cells and cells acclimated to this extreme light (EL). The results suggest that genetic or epigenetic variation, developing during maintenance of the population in moderate light, contributes to the acclimation capability. EL acclimation was associated with a high carotenoid-to-chlorophyll ratio and slowed down PSII charge recombination reactions, probably by affecting the pre-exponential Arrhenius factor of the rate constant. In agreement with these findings, EL acclimated cells showed only one tenth of the 1O2 level of control cells. In spite of low 1O2 levels, the rate of the damaging reaction of PSII photoinhibition was similar in EL acclimated and control cells. Furthermore, EL acclimation was associated with slow PSII electron transfer to artificial quinone acceptors. The data show that ability to grow and thrive in extremely strong light is not restricted to photoinhibition-resistant organisms such as Chlorella ohadii or to high-light tolerant mutants, but a wild-type strain of a common model microalga has this ability as well.


Asunto(s)
Aclimatación/efectos de la radiación , Chlamydomonas reinhardtii/fisiología , Fotosíntesis/efectos de la radiación , Complejo de Proteína del Fotosistema I/efectos de la radiación , Complejo de Proteína del Fotosistema II/efectos de la radiación , Carotenoides/análisis , Carotenoides/efectos de la radiación , Chlamydomonas reinhardtii/crecimiento & desarrollo , Chlamydomonas reinhardtii/efectos de la radiación , Clorofila/análisis , Clorofila/efectos de la radiación , Transporte de Electrón/efectos de la radiación , Oxígeno/metabolismo , Fenotipo , Plastoquinona/análisis , Oxígeno Singlete/metabolismo , Tilacoides/metabolismo
7.
Plant Cell Environ ; 44(3): 747-761, 2021 03.
Artículo en Inglés | MEDLINE | ID: mdl-33215722

RESUMEN

Long-term fluctuating light (FL) conditions are very common in natural environments. The physiological and biochemical mechanisms for acclimation to FL differ between species. However, most of the current conclusions regarding acclimation to FL were made based on studies in algae or Arabidopsis thaliana. It is still unclear how rice (Oryza sativa L.) integrate multiple physiological changes to acclimate to long-term FL. In this study, we found that rice growth was repressed under long-term FL. By systematically measuring phenotypes and physiological parameters, we revealed that: (a) under short-term FL, photosystem I (PSI) was inhibited, while after 1-7 days of long-term FL, both PSI and PSII were inhibited. Higher acceptor-side limitation in electron transport and higher overall nonphotochemical quenching (NPQ) explained the lower efficiencies of PSI and PSII, respectively. (b) An increase in pH differences across the thylakoid membrane and a decrease in thylakoid proton conductivity revealed a reduction of ATP synthase activity. (c) Using electron microscopy, we showed a decrease in membrane stacking and stomatal opening after 7 days of FL treatment. Taken together, our results show that electron flow, ATP synthase activity and NPQ regulation are the major processes determining the growth performance of rice under long-term FL conditions.


Asunto(s)
Aclimatación/efectos de la radiación , Oryza/efectos de la radiación , Fotosíntesis/efectos de la radiación , Clorofila/metabolismo , Luz , Oryza/anatomía & histología , Oryza/crecimiento & desarrollo , Oryza/fisiología , Complejo de Proteína del Fotosistema I/metabolismo , Complejo de Proteína del Fotosistema I/efectos de la radiación , Complejo de Proteína del Fotosistema II/metabolismo , Complejo de Proteína del Fotosistema II/efectos de la radiación , Tilacoides/metabolismo , Tilacoides/efectos de la radiación
8.
Chemistry ; 27(9): 3013-3018, 2021 Feb 10.
Artículo en Inglés | MEDLINE | ID: mdl-32743875

RESUMEN

Photosystem I (PS I) is a transmembrane protein that assembles perpendicular to the membrane, and performs light harvesting, energy transfer, and electron transfer to a final, water-soluble electron acceptor. We present here a supramolecular model of it formed by a bicationic oligofluorene 12+ bound to the bisanionic photoredox catalyst eosin Y (EY2- ) in phospholipid bilayers. According to confocal microscopy, molecular modeling, and time dependent density functional theory calculations, 12+ prefers to align perpendicularly to the lipid bilayer. In presence of EY2- , a strong complex is formed (Ka =2.1±0.1×106 m-1 ), which upon excitation of 12+ leads to efficient energy transfer to EY2- . Follow-up electron transfer from the excited state of EY2- to the water-soluble electron donor EDTA was shown via UV-Vis absorption spectroscopy. Overall, controlled self-assembly and photochemistry within the membrane provides an unprecedented yet simple synthetic functional mimic of PS I.


Asunto(s)
Transferencia de Energía/efectos de la radiación , Luz , Membrana Dobles de Lípidos/química , Membrana Dobles de Lípidos/efectos de la radiación , Fosfolípidos/química , Fosfolípidos/efectos de la radiación , Complejo de Proteína del Fotosistema I/efectos de la radiación , Transporte de Electrón/efectos de la radiación , Fotoquímica
9.
Plant Sci ; 301: 110655, 2020 Dec.
Artículo en Inglés | MEDLINE | ID: mdl-33218624

RESUMEN

We demonstrated the existence of PSI-LHCI-LHCII-Lhcb4 supercomplexes and PSI-LHCI-PSII-LHCII megacomplexes in the stroma lamellae and grana margins of maize mesophyll chloroplasts; these complexes consist of different LHCII trimers and monomer antenna proteins per PSI photocentre. These complexes are formed in both low (LL) and high (HL) light growth conditions, but with different contents. We attempted to identify the components and structure of these complexes in maize chloroplasts isolated from the leaves of low and high light-grown plants after darkness and transition to far red (FR) light of high intensity. Exposition of plants from high and low light growth condition on FR light induces different rearrangements in the composition of super- and megacomplexes. During FR light exposure, in plants from LL, the PSI-LHCI-LHCII-Lhcb4 supercomplex dissociates into free LHCII-Lhcb4 and PSI-LHCI complexes, and these complexes associate with the PSII monomer. This process occurs differently in plants from HL. Exposition to FR light causes dissociation of both PSI-LHCI-LHCII-Lhcb4 supercomplexes and PSI-PSII megacomplexes. These results suggest a different function of super- and megacomplex organization than the classic state transitions model, which assumes that the movement of LHCII trimers in the thylakoid membraneis considered as a mechanism for balancing light absorption between the two photosystems in light stress. The behavior of the complexes described in this article does not seem to be well explained by this model, i.e., it does not seem likely that the primary purpose of these megacomplexes dynamics is to balance excitation pressure. Rather, as stated in this article, it seems to indicate a role of these complexes for PSI in excitation quenching and for PSII in turnover.


Asunto(s)
Complejos de Proteína Captadores de Luz/efectos de la radiación , Complejo de Proteína del Fotosistema I/efectos de la radiación , Complejo de Proteína del Fotosistema II/efectos de la radiación , Zea mays/efectos de la radiación , Cloroplastos/metabolismo , Cloroplastos/efectos de la radiación , Oscuridad , Luz , Complejos de Proteína Captadores de Luz/metabolismo , Células del Mesófilo/metabolismo , Células del Mesófilo/efectos de la radiación , Complejo de Proteína del Fotosistema I/metabolismo , Complejo de Proteína del Fotosistema II/metabolismo , Hojas de la Planta/fisiología , Hojas de la Planta/efectos de la radiación , Tilacoides/metabolismo , Tilacoides/efectos de la radiación , Zea mays/fisiología
10.
Plant J ; 104(4): 1088-1104, 2020 11.
Artículo en Inglés | MEDLINE | ID: mdl-32889743

RESUMEN

The plastoquinone (PQ) pool mediates electron flow and regulates photoacclimation in plants. Here we report the action spectrum of the redox state of the PQ pool in Arabidopsis thaliana, showing that 470-500, 560 or 650-660 nm light favors Photosystem II (PSII) and reduces the PQ pool, whereas 420-440, 520 or 690 nm light favors Photosystem I (PSI) and oxidizes PQ. These data were used to construct a model predicting the redox state of PQ from the spectrum of any polychromatic light source. Moderate reduction of the PQ pool induced transition to light state 2, whereas state 1 required highly oxidized PQ. In low-intensity PSI light, PQ was more oxidized than in darkness and became gradually reduced with light intensity, while weak PSII light strongly reduced PQ. Natural sunlight was found to favor PSI, which enables plants to use the redox state of the PQ pool as a measure of light intensity.


Asunto(s)
Arabidopsis/fisiología , Plastoquinona/metabolismo , Aclimatación , Espectro de Acción , Arabidopsis/efectos de la radiación , Oscuridad , Luz , Oxidación-Reducción , Complejo de Proteína del Fotosistema I/metabolismo , Complejo de Proteína del Fotosistema I/efectos de la radiación , Complejo de Proteína del Fotosistema II/metabolismo , Complejo de Proteína del Fotosistema II/efectos de la radiación , Plastoquinona/efectos de la radiación
11.
Sci Rep ; 10(1): 6770, 2020 04 21.
Artículo en Inglés | MEDLINE | ID: mdl-32317747

RESUMEN

Although light is essential for photosynthesis, when in excess, it may damage the photosynthetic apparatus, leading to a phenomenon known as photoinhibition. Photoinhibition was thought as a light-induced damage to photosystem II; however, it is now clear that even photosystem I may become very vulnerable to light. One main characteristic of light induced damage to photosystem II (PSII) is the increased turnover of the reaction center protein, D1: when rate of degradation exceeds the rate of synthesis, loss of PSII activity is observed. With respect to photosystem I (PSI), an excess of electrons, instead of an excess of light, may be very dangerous. Plants possess a number of mechanisms able to prevent, or limit, such damages by safe thermal dissipation of light energy (non-photochemical quenching, NPQ), slowing-down of electron transfer through the intersystem transport chain (photosynthesis-control, PSC) in co-operation with the Proton Gradient Regulation (PGR) proteins, PGR5 and PGRL1, collectively called as short-term photoprotection mechanisms, and the redistribution of light between photosystems, called state transitions (responsible of fluorescence quenching at PSII, qT), is superimposed to these short term photoprotective mechanisms. In this manuscript we have generated a number of higher order mutants by crossing genotypes carrying defects in each of the short-term photoprotection mechanisms, with the final aim to obtain a direct comparison of their role and efficiency in photoprotection. We found that mutants carrying a defect in the ΔpH-dependent photosynthesis-control are characterized by photoinhibition of both photosystems, irrespectively of whether PSBS-dependent NPQ or state transitions defects were present or not in the same individual, demonstrating the primary role of PSC in photoprotection. Moreover, mutants with a limited capability to develop a strong PSBS-dependent NPQ, were characterized by a high turnover of the D1 protein and high values of Y(NO), which might reflect energy quenching processes occurring within the PSII reaction center.


Asunto(s)
Proteínas de Arabidopsis/genética , Proteínas de la Membrana/genética , Proteínas del Complejo del Centro de Reacción Fotosintética/genética , Complejo de Proteína del Fotosistema I/genética , Complejo de Proteína del Fotosistema II/genética , Arabidopsis/genética , Arabidopsis/fisiología , Genotipo , Concentración de Iones de Hidrógeno , Luz , Fotosíntesis/genética , Fotosíntesis/efectos de la radiación , Complejo de Proteína del Fotosistema I/efectos de la radiación , Complejo de Proteína del Fotosistema II/efectos de la radiación
12.
Photosynth Res ; 144(3): 373-382, 2020 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-32333230

RESUMEN

Moderate heat stress and fluctuating light are typical conditions in summer in tropical and subtropical regions. This type of stress can cause photodamage to photosystems I and II (PSI and PSII). However, photosynthetic responses to the combination of heat and fluctuating light in young leaves are little known. In this study, we investigated chlorophyll fluorescence and P700 redox state under fluctuating light at 25 °C and 42 °C in young leaves of tobacco. Our results indicated that fluctuating light caused selective photodamage to PSI in the young leaves at 25 °C and 42 °C. Furthermore, the moderate heat stress significantly accelerated photoinhibition of PSI under fluctuating light. Within the first 10 s after transition from low to high light, cyclic electron flow (CEF) around PSI was highly stimulated at 25 °C but was slightly activated at 42 °C. Such depression of CEF activation at moderate heat stress were unable to maintain energy balance under high light. As a result, electron flow from PSI to NADP+ was restricted, leading to the over-reduction of PSI electron carriers. These results indicated that moderate heat stress altered the CEF performance under fluctuating light and thus accelerated PSI photoinhibition in tobacco young leaves.


Asunto(s)
Transporte de Electrón/efectos de la radiación , Nicotiana/fisiología , Fotosíntesis/efectos de la radiación , Complejo de Proteína del Fotosistema I/metabolismo , Respuesta al Choque Térmico , Luz , Oxidación-Reducción , Complejo de Proteína del Fotosistema I/efectos de la radiación , Complejo de Proteína del Fotosistema II/metabolismo , Complejo de Proteína del Fotosistema II/efectos de la radiación , Hojas de la Planta/fisiología , Hojas de la Planta/efectos de la radiación , Nicotiana/efectos de la radiación
13.
Langmuir ; 36(16): 4556-4562, 2020 04 28.
Artículo en Inglés | MEDLINE | ID: mdl-32239960

RESUMEN

In biological systems, membrane proteins play major roles in energy conversion, transport, sensing, and signal transduction. Of special interest are the photosynthetic reaction centers involved in the initial process of light energy conversion to electrical and chemical energies. The oriented binding of membrane proteins to solid surfaces is important for biotechnological applications. In some cases, novel properties are generated as a result of the interaction between proteins and solid surfaces. We developed a novel approach for the oriented tagging of membrane proteins. In this unique process, bifunctional molecules are used to chemically tag the exposed surfaces of membrane proteins at selected sides of membrane vesicles. The isolated tagged membrane proteins were self-assembled on solid surfaces, leading to the fabrication of dens-oriented layers on metal and glass surfaces, as seen from the atomic force microscopy (AFM) images. In this work, we used chromatophores and membrane vesicles containing protein chlorophyll complexes for the isolation of the bacterial reaction center and photosystem I, from photosynthetic bacteria and cyanobacteria, respectively. The oriented layers, which were fabricated on metal surfaces, were functional and generated light-induced photovoltage that was measured by the Kalvin probe apparatus. The polarity of the photovoltage depended on the orientation of proteins in the layers. Other membrane proteins can be tagged by the same method. However, we preferred the use of reaction centers because their orientation can be easily detected by the polarity of their photovoltages.


Asunto(s)
Proteínas Bacterianas/química , Proteínas Inmovilizadas/química , Complejo de Proteína del Fotosistema I/química , Proteínas Bacterianas/efectos de la radiación , Reactivos de Enlaces Cruzados/química , Electroquímica , Oro/química , Proteínas Inmovilizadas/efectos de la radiación , Luz , Liposomas/química , Complejo de Proteína del Fotosistema I/efectos de la radiación , Rhodobacter/enzimología , Succinimidas/química , Synechocystis/enzimología
14.
Nat Commun ; 11(1): 238, 2020 01 13.
Artículo en Inglés | MEDLINE | ID: mdl-31932639

RESUMEN

Chlorophylls (Chl) play pivotal roles in energy capture, transfer and charge separation in photosynthesis. Among Chls functioning in oxygenic photosynthesis, Chl f is the most red-shifted type first found in a cyanobacterium Halomicronema hongdechloris. The location and function of Chl f in photosystems are not clear. Here we analyzed the high-resolution structures of photosystem I (PSI) core from H. hongdechloris grown under white or far-red light by cryo-electron microscopy. The structure showed that, far-red PSI binds 83 Chl a and 7 Chl f, and Chl f are associated at the periphery of PSI but not in the electron transfer chain. The appearance of Chl f is well correlated with the expression of PSI genes induced under far-red light. These results indicate that Chl f functions to harvest the far-red light and enhance uphill energy transfer, and changes in the gene sequences are essential for the binding of Chl f.


Asunto(s)
Clorofila/análogos & derivados , Complejo de Proteína del Fotosistema I/química , Complejo de Proteína del Fotosistema I/metabolismo , Sitios de Unión , Clorofila/metabolismo , Clorofila/efectos de la radiación , Clorofila A/metabolismo , Clorofila A/efectos de la radiación , Microscopía por Crioelectrón , Cianobacterias/química , Cianobacterias/fisiología , Transferencia de Energía , Luz , Modelos Moleculares , Complejo de Proteína del Fotosistema I/efectos de la radiación , Conformación Proteica
15.
Plant Cell Physiol ; 61(1): 41-52, 2020 Jan 01.
Artículo en Inglés | MEDLINE | ID: mdl-31511895

RESUMEN

In nature, photosynthetic organisms are exposed to highly dynamic environmental conditions where the excitation energy and electron flow in the photosynthetic apparatus need to be continuously modulated. Fluctuations in incident light are particularly challenging because they drive oversaturation of photosynthesis with consequent oxidative stress and photoinhibition. Plants and algae have evolved several mechanisms to modulate their photosynthetic machinery to cope with light dynamics, such as thermal dissipation of excited chlorophyll states (non-photochemical quenching, NPQ) and regulation of electron transport. The regulatory mechanisms involved in the response to light dynamics have adapted during evolution, and exploring biodiversity is a valuable strategy for expanding our understanding of their biological roles. In this work, we investigated the response to fluctuating light in Nannochloropsis gaditana, a eukaryotic microalga of the phylum Heterokonta originating from a secondary endosymbiotic event. Nannochloropsis gaditana is negatively affected by light fluctuations, leading to large reductions in growth and photosynthetic electron transport. Exposure to light fluctuations specifically damages photosystem I, likely because of the ineffective regulation of electron transport in this species. The role of NPQ, also assessed using a mutant strain specifically depleted of this response, was instead found to be minor, especially in responding to the fastest light fluctuations.


Asunto(s)
Luz , Fotosíntesis/fisiología , Estramenopilos/metabolismo , Simbiosis/fisiología , Biodiversidad , Transporte de Electrón/fisiología , Estrés Oxidativo , Complejo de Proteína del Fotosistema I/metabolismo , Complejo de Proteína del Fotosistema I/efectos de la radiación , Plantas/metabolismo , Estramenopilos/crecimiento & desarrollo , Estramenopilos/efectos de la radiación
16.
Plant Sci ; 287: 110166, 2019 Oct.
Artículo en Inglés | MEDLINE | ID: mdl-31481226

RESUMEN

In angiosperms, cyclic electron flow (CEF) around photosystem I (PSI) is more important for photoprotection under fluctuating light than under constant light. However, the underlying mechanism is not well known. In the present study, we measured the CEF activity, P700 redox state and electrochromic shift signal upon a sudden transition from low to high light in wild-type plants of Arabidopsis thaliana and Bletilla striata (Orchidaceae). Within the first 20 s after transition from low to high light, P700 was highly reduced in both species, which was accompanied with a sufficient proton gradient (ΔpH) across the thylakoid membranes. Meanwhile, the level of CEF activation was elevated. After transition from low to high light for 60 s, the plants generated an optimal ΔpH. Under such condition, PSI was highly oxidized and the level of CEF activation decreased to the steady state. Furthermore, the CEF activation was positively correlated to the P700 reduction ratio. These results indicated that upon a sudden transition from low to high light, the insufficient ΔpH led to the over-reduction of PSI electron carriers, which in turn stimulated the CEF around PSI. This transient stimulation of CEF not only favored the rapid ΔpH formation but also accepted electrons from PSI, thus protecting PSI at donor and acceptor sides. These findings provide new insights into the important role of CEF in regulation of photosynthesis under fluctuating light.


Asunto(s)
Arabidopsis/metabolismo , Transporte de Electrón , Orchidaceae/metabolismo , Complejo de Proteína del Fotosistema I/metabolismo , Arabidopsis/efectos de la radiación , Clorofila/metabolismo , Relación Dosis-Respuesta en la Radiación , Transporte de Electrón/efectos de la radiación , Luz , Orchidaceae/efectos de la radiación , Complejo de Proteína del Fotosistema I/efectos de la radiación
17.
Biochim Biophys Acta Bioenerg ; 1860(8): 651-658, 2019 08 01.
Artículo en Inglés | MEDLINE | ID: mdl-31299182

RESUMEN

Light drives photosynthesis. In plants it is absorbed by light-harvesting antenna complexes associated with Photosystem I (PSI) and photosystem II (PSII). As PSI and PSII work in series, it is important that the excitation pressure on the two photosystems is balanced. When plants are exposed to illumination that overexcites PSII, a special pool of the major light-harvesting complex LHCII is phosphorylated and moves from PSII to PSI (state 2). If instead PSI is over-excited the LHCII complex is dephosphorylated and moves back to PSII (state 1). Recent findings have suggested that LHCII might also transfer energy to PSI in state 1. In this work we used a combination of biochemistry and (time-resolved) fluorescence spectroscopy to investigate the PSI antenna size in state 1 and state 2 for Arabidopsis thaliana. Our data shows that 0.7 ± 0.1 unphosphorylated LHCII trimers per PSI are present in the stroma lamellae of state-1 plants. Upon transition to state 2 the antenna size of PSI in the stroma membrane increases with phosphorylated LHCIIs to a total of 1.2 ± 0.1 LHCII trimers per PSI. Both phosphorylated and unphosphorylated LHCII function as highly efficient PSI antenna.


Asunto(s)
Arabidopsis/enzimología , Complejos de Proteína Captadores de Luz/fisiología , Luz , Complejo de Proteína del Fotosistema I/efectos de la radiación , Arabidopsis/ultraestructura , Digitonina/farmacología , Transferencia de Energía , Complejos de Proteína Captadores de Luz/efectos de los fármacos , Fosforilación , Complejo de Proteína del Fotosistema II/efectos de la radiación , Espectrometría de Fluorescencia
18.
Biochemistry ; 58(25): 2844-2852, 2019 06 25.
Artículo en Inglés | MEDLINE | ID: mdl-31145583

RESUMEN

The light-harvesting 1 reaction center (LH1-RC) complex in the purple sulfur bacterium Thiorhodovibrio ( Trv.) strain 970 cells exhibits its LH1 Q y transition at 973 nm, the lowest-energy Q y absorption among purple bacteria containing bacteriochlorophyll a (BChl a). Here we characterize the origin of this extremely red-shifted Q y transition. Growth of Trv. strain 970 did not occur in cultures free of Ca2+, and elemental analysis of Ca2+-grown cells confirmed that purified Trv. strain 970 LH1-RC complexes contained Ca2+. The LH1 Q y band of Trv. strain 970 was blue-shifted from 959 to 875 nm upon Ca2+ depletion, but the original spectral properties were restored upon Ca2+ reconstitution, which also occurs with the thermophilic purple bacterium Thermochromatium ( Tch.) tepidum. The amino acid sequences of the LH1 α- and ß-polypeptides from Trv. strain 970 closely resemble those of Tch. tepidum; however, Ca2+ binding in the Trv. strain 970 LH1-RC occurred more selectively than in Tch. tepidum LH1-RC and with a reduced affinity. Ultraviolet resonance Raman analysis indicated that the number of hydrogen-bonding interactions between BChl a and LH1 proteins of Trv. strain 970 was significantly greater than for Tch. tepidum and that Ca2+ was indispensable for maintaining these bonds. Furthermore, perfusion-induced Fourier transform infrared analyses detected Ca2+-induced conformational changes in the binding site closely related to the unique spectral properties of Trv. strain 970. Collectively, our results reveal an ecological strategy employed by Trv. strain 970 of integrating Ca2+ into its LH1-RC complex to extend its light-harvesting capacity to regions of the near-infrared spectrum unused by other purple bacteria.


Asunto(s)
Proteínas Bacterianas/metabolismo , Calcio/metabolismo , Complejos de Proteína Captadores de Luz/metabolismo , Complejo de Proteína del Fotosistema I/metabolismo , Proteínas Bacterianas/efectos de la radiación , Bacterioclorofila A/química , Bacterioclorofila A/metabolismo , Chromatiaceae/química , Chromatiaceae/crecimiento & desarrollo , Luz , Complejos de Proteína Captadores de Luz/efectos de la radiación , Conformación Molecular , Complejo de Proteína del Fotosistema I/efectos de la radiación , Procesos Fototróficos/efectos de la radiación , Unión Proteica , Estabilidad Proteica
19.
Photosynth Res ; 141(2): 151-163, 2019 Aug.
Artículo en Inglés | MEDLINE | ID: mdl-30710189

RESUMEN

Certain cyanobacteria can thrive in environments enriched in far-red light (700-800 nm) due to an acclimation process known as far-red light photoacclimation (FaRLiP). During FaRLiP, about 8% of the Chl a molecules in the photosystems are replaced by Chl f and a very small amount of Chl d. We investigated the spectroscopic properties of Photosystem I (PSI) complexes isolated from wild-type (WT) Synechococcus sp. PCC 7335 and a chlF mutant strain (lacking Chl f synthase) grown in white and far-red light (WL-PSI and FRL-PSI, respectively). WT-FRL-PSI complexes contain Chl f and Chl a but not Chl d. The light-minus dark difference spectrum of the trapping center at high spectral resolution indicates that the special pair in WT-FRL-PSI consists of Chl a molecules with maximum bleaching at 703-704 nm. The action spectrum for photobleaching of the special pair showed that Chl f molecules absorbing at wavelengths up to 800 nm efficiently transfer energy to the trapping center in FRL-PSI complexes to produce a charge-separated state. This is ~ 50 nm further into the near IR than WL-PSI; Chl f has a quantum yield equivalent to that of Chl a in the antenna, i.e., ~ 1.0. PSI complexes from Synechococcus 7002 carrying 3.8 Chl f molecules could promote photobleaching of the special pair by energy transfer at wavelengths longer than WT PSI complexes. Results from these latter studies are directly relevant to the issue of whether introduction of Chl f synthase into plants could expand the wavelength range available for oxygenic photosynthesis in crop plants.


Asunto(s)
Transferencia de Energía , Fotosíntesis/efectos de la radiación , Complejo de Proteína del Fotosistema I/metabolismo , Synechococcus/fisiología , Aclimatación , Clorofila/análogos & derivados , Clorofila/metabolismo , Luz , Complejo de Proteína del Fotosistema I/efectos de la radiación , Synechococcus/efectos de la radiación
20.
Photosynth Res ; 139(1-3): 145-154, 2019 Mar.
Artículo en Inglés | MEDLINE | ID: mdl-29808364

RESUMEN

Oxygenic photosynthetic organisms perform photosynthesis efficiently by distributing captured light energy to photosystems (PSs) at an appropriate balance. Maintaining photosynthetic efficiency under changing light conditions requires modification of light-harvesting and energy-transfer processes. In the current study, we examined how green algae regulate their light-harvesting functions in response to different light qualities. We measured low-temperature time-resolved fluorescence spectra of unicellular green algae Chlamydomonas reinhardtii and Chlorella variabilis cells grown under different light qualities. By observing the delayed fluorescence spectra, we demonstrated that both types of green algae primarily modified the associations between light-harvesting chlorophyll protein complexes (LHCs) and PSs (PSII and PSI). Under blue light, Chlamydomonas transferred more energy from LHC to chlorophyll (Chl) located far from the PSII reaction center, while energy was transferred from LHC to PSI via different energy-transfer pathways in Chlorella. Under green light, both green algae exhibited enhanced energy transfer from LHCs to both PSs. Red light induced fluorescence quenching within PSs in Chlamydomonas and LHCs in Chlorella. In Chlorella, energy transfer from PSII to PSI appears to play an important role in balancing excitation between PSII and PSI.


Asunto(s)
Chlorella/metabolismo , Luz , Chlorella/efectos de la radiación , Transferencia de Energía/efectos de la radiación , Fotosíntesis/efectos de la radiación , Complejo de Proteína del Fotosistema I/metabolismo , Complejo de Proteína del Fotosistema I/efectos de la radiación , Complejo de Proteína del Fotosistema II/metabolismo , Complejo de Proteína del Fotosistema II/efectos de la radiación
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