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Biochimica Et Biophysica Acta Aug 2011Because life on earth is governed by the second law of thermodynamics, it is subject to increasing entropy. Oxygenic photosynthesis, the earth's major producer of both... (Review)
Review
Because life on earth is governed by the second law of thermodynamics, it is subject to increasing entropy. Oxygenic photosynthesis, the earth's major producer of both oxygen and organic matter, is a principal player in the development and maintenance of life, and thus results in increased order. The primary steps of oxygenic photosynthesis are driven by four multi-subunit membrane protein complexes: photosystem I, photosystem II, cytochrome b(6)f complex, and F-ATPase. Photosystem II generates the most positive redox potential found in nature and thus capable of extracting electrons from water. Photosystem I generates the most negative redox potential found in nature; thus, it largely determines the global amount of enthalpy in living systems. The recent structural determination of PSII and PSI complexes from cyanobacteria and plants sheds light on the evolutionary forces that shaped oxygenic photosynthesis. This newly available structural information complements knowledge gained from genomic and proteomic data, allowing for a more precise description of the scenario in which the evolution of life systems took place. This article is part of a Special Issue entitled: Regulation of Electron Transport in Chloroplasts.
Topics: Adenosine Triphosphatases; Bacterial Proteins; Cyanobacteria; Cytochrome b6f Complex; Oxidation-Reduction; Oxygen; Photosynthesis; Photosystem I Protein Complex; Photosystem II Protein Complex; Plant Proteins; Plants
PubMed: 20955682
DOI: 10.1016/j.bbabio.2010.10.011 -
Scientific Reports Apr 2020Although light is essential for photosynthesis, when in excess, it may damage the photosynthetic apparatus, leading to a phenomenon known as photoinhibition....
Higher order photoprotection mutants reveal the importance of ΔpH-dependent photosynthesis-control in preventing light induced damage to both photosystem II and photosystem I.
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.
Topics: Arabidopsis; Arabidopsis Proteins; Genotype; Hydrogen-Ion Concentration; Light; Membrane Proteins; Photosynthesis; Photosynthetic Reaction Center Complex Proteins; Photosystem I Protein Complex; Photosystem II Protein Complex
PubMed: 32317747
DOI: 10.1038/s41598-020-62717-1 -
Plant Science : An International... Mar 2020Moderate heat stress is usually accompanied with fluctuating light in summer. Although either heat stress or fluctuating light can cause photoinhibition of photosystems...
Moderate heat stress is usually accompanied with fluctuating light in summer. Although either heat stress or fluctuating light can cause photoinhibition of photosystems I and II (PSI and PSII), it is unclear whether moderate heat stress accelerate photoinhibition under fluctuating light. Here, we measured chlorophyll fluorescence, P700 redox state and the electrochromic shift signal under fluctuating light at 25 °C and 42 °C for tobacco leaves. We found that (1) the thylakoid proton conductance was significantly enhanced at 42 °C, leading to a decline in trans-thylakoid proton gradient (ΔpH); (2) this low ΔpH at 42 °C did not decrease donor-side limitation of PSI and thermal energy dissipation in PSII; (3) the activation of cyclic electron flow (CEF) around PSI was elevated at 42 °C; and (4) the moderate heat stress did not accelerate photoinhibition of PSI and PSII under fluctuating light. These results strongly indicate that under moderate heat stress the stimulation of CEF protects PSI under fluctuating light in tobacco leaves.
Topics: Heat-Shock Response; Light; Photosystem I Protein Complex; Photosystem II Protein Complex; Plant Leaves; Nicotiana
PubMed: 32005377
DOI: 10.1016/j.plantsci.2019.110371 -
Toxics Aug 2022Mercury (Hg) poses high toxicity to organisms including algae. Studies showed that the growth and photosynthesis of green algae such as Chlorella are vulnerable to Hg...
Mercury (Hg) poses high toxicity to organisms including algae. Studies showed that the growth and photosynthesis of green algae such as Chlorella are vulnerable to Hg stress. However, the differences between the activities and tolerance of photosystem I and II (PSI and PSII) of green microalgae under Hg exposure are still little known. Responses of quantum yields and electron transport rates (ETRs) of PSI and PSII of Chlorella pyrenoidosa to 0.05−1 mg/L Hg2+ were simultaneously measured for the first time by using the Dual-PAM-100 system. The photosystems were isolated to analyze the characteristics of toxicity of Hg during the binding process. The inhibition of Hg2+ on growth and photosystems was found. PSII was more seriously affected by Hg2+ than PSI. After Hg2+ exposure, the photochemical quantum yield of PSII [Y(II)] decreased with the increase in non-photochemical fluorescence quenching [Y(NO) and Y(NPQ)]. The toxic effects of Hg on the photochemical quantum yield and ETR in PSI were lower than those of PSII. The stimulation of cyclic electron yield (CEF) was essential for the stability and protection of PSI under Hg stress and played an important role in the induction of non-photochemical quenching (NPQ). The results showed a strong combination ability of Hg ions and photosystem particles. The number of the binding sites (n) of Hg on PSII was more than that of PSI, which may explain the different toxicity of Hg on PSII and PSI.
PubMed: 36006134
DOI: 10.3390/toxics10080455 -
The Plant Journal : For Cell and... Apr 2020The biological conversion of light energy into chemical energy is performed by a flexible photosynthetic machinery located in the thylakoid membranes. Photosystems I and...
The biological conversion of light energy into chemical energy is performed by a flexible photosynthetic machinery located in the thylakoid membranes. Photosystems I and II (PSI and PSII) are the two complexes able to harvest light. PSI is the last complex of the electron transport chain and is composed of multiple subunits: the proteins building the catalytic core complex that are well conserved between oxygenic photosynthetic organisms, and, in green organisms, the membrane light-harvesting complexes (Lhc) necessary to increase light absorption. In plants, four Lhca proteins (Lhca1-4) make up the antenna system of PSI, which can be further extended to optimize photosynthesis by reversible binding of LHCII, the main antenna complex of photosystem II. Here, we used biochemistry and electron microscopy in Arabidopsis to reveal a previously unknown supercomplex of PSI with LHCII that contains an additional Lhca1-a4 dimer bound on the PsaB-PsaI-PsaH side of the complex. This finding contradicts recent structural studies suggesting that the presence of an Lhca dimer at this position is an exclusive feature of algal PSI. We discuss the features of the additional Lhca dimer in the large plant PSI-LHCII supercomplex and the differences with the algal PSI. Our work provides further insights into the intricate structural plasticity of photosystems.
Topics: Arabidopsis; Arabidopsis Proteins; Chlorophyll Binding Proteins; Electron Transport Chain Complex Proteins; Microscopy, Electron; Phosphorylation; Photosynthesis; Photosystem I Protein Complex; Photosystem II Protein Complex; Thylakoids
PubMed: 31811681
DOI: 10.1111/tpj.14634 -
Small (Weinheim An Der Bergstrasse,... Sep 2013Layered assemblies of photosystem I, PSI, and/or photosystem II, PSII, on ITO electrodes are constructed using a layer-by-layer deposition process, where poly...
Layered assemblies of photosystem I, PSI, and/or photosystem II, PSII, on ITO electrodes are constructed using a layer-by-layer deposition process, where poly N,N'-dibenzyl-4,4'-bipyridinium (poly-benzyl viologen, PBV(2+) ) is used as an inter-protein "glue". While the layered assembly of PSI generates an anodic photocurrent only in the presence of a sacrificial electron donor system, such as dichlorophenol indophenol (DCPIP)/ascorbate, the PSII-modified electrode leads, upon irradiation, to the formation of an anodic photocurrent (while evolving oxygen), in the absence of any sacrificial component. The photocurrent is generated by transferring the electrons from the PSII units to the PBV(2+) redox polymer. The charge-separated species allow, then, the injection of the electrons to the electrode, with the concomitant evolution of O2 . A layered assembly, consisting of a PSI layer attached to a layer of PSII by the redox polymer PBV(2+) , leads to an anodic photocurrent that is 2-fold higher, as compared to the anodic photocurrent generated by a PSII-modified electrode. This observation is attributed to an enhanced charge separation in the two-photosystem assembly. By the further nano-engineering of the two photosystems on the electrode using two different redox polymers, vectorial electron transfer to the electrode is demonstrated, resulting in a ca. 6-fold enhancement in the photocurrent. The reversed bi-layer assembly, consisting of a PSII layer linked to a layer of PSI by the PBV(2+) redox polymer, yields, upon irradiation, an inefficient cathodic current. This observation is attributed to a mixture of photoinduced electron transfer reactions of opposing effects on the photocurrent directions in the two-photosystem assembly.
Topics: Light; Oxidation-Reduction; Photochemistry; Photosystem I Protein Complex; Photosystem II Protein Complex; Polymers
PubMed: 23606348
DOI: 10.1002/smll.201300051 -
Nature Feb 2001Oxygenic photosynthesis is the principal energy converter on earth. It is driven by photosystems I and II, two large protein-cofactor complexes located in the thylakoid...
Oxygenic photosynthesis is the principal energy converter on earth. It is driven by photosystems I and II, two large protein-cofactor complexes located in the thylakoid membrane and acting in series. In photosystem II, water is oxidized; this event provides the overall process with the necessary electrons and protons, and the atmosphere with oxygen. To date, structural information on the architecture of the complex has been provided by electron microscopy of intact, active photosystem II at 15-30 A resolution, and by electron crystallography on two-dimensional crystals of D1-D2-CP47 photosystem II fragments without water oxidizing activity at 8 A resolution. Here we describe the X-ray structure of photosystem II on the basis of crystals fully active in water oxidation. The structure shows how protein subunits and cofactors are spatially organized. The larger subunits are assigned and the locations and orientations of the cofactors are defined. We also provide new information on the position, size and shape of the manganese cluster, which catalyzes water oxidation.
Topics: Chlorophyll; Chlorophyll A; Crystallography, X-Ray; Cyanobacteria; Light-Harvesting Protein Complexes; Manganese; Models, Molecular; Photosynthetic Reaction Center Complex Proteins; Photosystem II Protein Complex; Protein Conformation
PubMed: 11217865
DOI: 10.1038/35055589 -
The New Phytologist Nov 2020Photosystems I and II are the central components of the solar energy conversion machinery in oxygenic photosynthesis. They are large functional units embedded in the... (Review)
Review
Photosystems I and II are the central components of the solar energy conversion machinery in oxygenic photosynthesis. They are large functional units embedded in the photosynthetic membranes, where they harvest light and use its energy to drive electrons from water to NADPH. Their composition and organization change in response to different environmental conditions, making these complexes dynamic units. Some of the interactions between subunits survive purification, resulting in the well-defined structures that were recently resolved by cryo-electron microscopy. Other interactions instead are weak, preventing the possibility of isolating and thus studying these complexes in vitro. This review focuses on these supercomplexes of vascular plants, which at the moment cannot be 'seen' but that represent functional units in vivo.
Topics: Cryoelectron Microscopy; Electrons; Light-Harvesting Protein Complexes; Oxygen; Photosynthesis; Photosystem I Protein Complex; Photosystem II Protein Complex
PubMed: 32562266
DOI: 10.1111/nph.16758 -
Biochimica Et Biophysica Acta Jul 1975A model for the photochemical apparatus of photosynthesis is presented which accounts for the fluorescence properties of Photosystem II and Photosystem I as well as...
A model for the photochemical apparatus of photosynthesis is presented which accounts for the fluorescence properties of Photosystem II and Photosystem I as well as energy transfer between the two photosystems. The model was tested by measuring at - 196 degrees C fluorescence induction curves at 690 and 730 nm in the absence and presence of 5mMMgCl2 which presumably changes the distrubution of excitation energy between the two photosystems. The equations describing the fluorescence properties involve terms for the distribution of absorbed quanta, alpha, being the fraction distributed to Photosystem I, and beta, the fraction to Photosystem II to Photosystem I, KT(II yields I). The data, analyzed within the context of the model, permit a direct comparison of alpha and kt(II yields I) in the absence (minus) and presence (+) of Mg-2+ :alpha minus/alpha-+ equals 1.2 and k-minus t)II yields I)/K-+T(II yields I) equal to 1.9. If the criterion that alpha + beta equal to 1 is applied absolute values can be calculated: in the presence of Mg-2+, alpha-+ equal to 0.27 and the yield of energy transfer, phi-+ t(II yields I) varied the presence of Mg-2+, alpha-+ equal to 0.27 and the yield of energy transfer, phi-+ t(II yields I) varied from 0.065 when the Photosystem II reaction centers were all open to 0.23 when they were closed. In the absence of Mg-2+, alpha-minus equal to 0.32 and phi t(II yields I) varied from 0.12 to 0.28. The data were also analyzed assuming that two types of energy transfer could be distinguished; a transfer from the light-harvesting chlorophyll of Photosystem II to Photosystem I, kt(II yields I), and a transfer from the reaction centers of Photosystem II to Photosystem I, kt(II yields I). In that case alpha-minus/alpha+ equal to 1.3, k-minus t(II yields I)/k+ t(II yields I)equal to 1.3 and k-minus t(II yields I) equal to 3.0. It was concluded, however, that both of these types of energy transfer are different manifestations of a single energy transfer process.
Topics: Chloroplasts; Energy Transfer; Kinetics; Magnesium; Mathematics; Models, Chemical; Oxidative Phosphorylation; Photophosphorylation; Plants; Spectrometry, Fluorescence; Time Factors
PubMed: 1148253
DOI: 10.1016/0005-2728(75)90190-5 -
Results and Problems in Cell... 2008Photosynthesis is the major process that converts solar energy into chemical energy on Earth. Two and a half billion years ago, the ancestors of cyanobacteria were able... (Review)
Review
Photosynthesis is the major process that converts solar energy into chemical energy on Earth. Two and a half billion years ago, the ancestors of cyanobacteria were able to use water as electron source for the photosynthetic process, thereby evolving oxygen and changing the atmosphere of our planet Earth. Two large membrane protein complexes, Photosystems I and II, catalyze the primary step in this energy conversion, the light-induced charge separation across the photosynthetic membrane. This chapter describes and compares the structure of two Photosystems and discusses their function in respect to the mechanism of light harvesting, electron transfer and water splitting.
Topics: Catalysis; Cyanobacteria; Earth, Planet; Electron Transport; Membrane Proteins; Models, Biological; Molecular Conformation; Oxygen; Photosynthesis; Photosystem I Protein Complex; Photosystem II Protein Complex; Plants; Protein Structure, Tertiary; Water; X-Rays
PubMed: 18066506
DOI: 10.1007/400_2007_044