During photosynthesis, two photoreaction centers located in the thylakoid membranes of the chloroplast, photosystems I and II (PSI and PSII), use light energy to mobilize electrons to generate ATP and NADPH. Different modes of electron flow exist, of which the linear electron flow is driven by PSI and PSII, generating ATP and NADPH, whereas the cyclic electron flow (CEF) only generates ATP and is driven by the PSI alone. Different environmental and metabolic conditions require the adjustment of ATP/NADPH ratios and a switch of electron distribution between the two photosystems. With the exception of PGR5, other components facilitating CEF are unknown. Here, we report the identification of PGRL1, a transmembrane protein present in thylakoids of Arabidopsis thaliana. Plants lacking PGRL1 show perturbation of CEF, similar to PGR5-deficient plants. We find that PGRL1 and PGR5 interact physically and associate with PSI. We therefore propose that the PGRL1-PGR5 complex facilitates CEF in eukaryotes.
. As shown in Extended Data Fig. 1a, an ECS signal is visible in P.tricornutum, the characteristics of which depend on the physiological conditions. Deconvolution of the ECS decay-associated spectra (DAS) (see Supplementary Information and Extended Data Fig. 1b,c) explains these observations by revealing the existence of two ECS components (Fig. 1a), respectively characterized by linear and quadratic responses to the ΔΨ (Fig. 1b). The existence of a quadratic ECS, predicted by theory 7 but observed to date only in green algae mutants (Fig. 1c), but was also suppressed by anaerobiosis or by pharmacological inhibition of mitochondrial activity (Fig. 1d, e). This suggests that the PMF is generated in the dark by the plastidial ATPase, which hydrolyses ATP of mitochondrial origin, as previously suggested in green algae 9 .In Viridiplantae (including green algae and higher plants), the AEPs generating additional ATP in the light comprise cyclic electron flow (CEF) around PS1 10 and the water-to-water cycles (WWC). uptake (U 0 ) increased with light, being ~2.5-fold higher at saturating light intensities than in the dark (Extended Data Fig. 2b, d). We further found that the light-stimulated consumption of oxygen was blocked by DCMU (Extended Data Fig. 2c, d), indicating that it was fed by electrons derived from PS2.Moreover, U 0 linearly increased with O 2 evolution, in agreement with earlier findings in the diatom Thalassiosira pseudonana 15, with a slope indicating that ~10% of the electron flow from PSII participate in WWC, regardless of light intensity (Fig 2b). These results indicate that WWC produces a constant extra ATP per photosynthetically-generated NADPH. This is expected for an AEP that contributes to optimizing CO 2 assimilation at any light intensity, and is not the case for CEF, which is completely insensitive to changes in the photosynthetic flux (LEF, Fig 2a).If this WWC is due to the export of photosynthetic products towards the mitochondrial oxidases, then any mitochondrial dysfunction should negatively affect photosynthetic electron transfer rates (ETR PSII ) and light-dependent growth. Mitochondrial respiration comprises a cyanidesensitive pathway (involving Complex III) and an insensitive pathway involving the alternative oxidase (AOX). We therefore modulated mitochondrial activity by adding increasing amounts of Antimycin A (AA) or myxothiazol (Mx), inhibitors of Complex III, in conditions where the AOX was inhibited by SHAM (see legend to Fig. 2d). Both the ΔΨ d and ETR PSII followed respiration linearly (Fig. 2c, d and Extended Data Fig. 3). The almost complete shut-down of respiration resulted in a decrease of photosynthesis which was independent of light intensity (Fig. 3b).Overall we found that in the dark a PMF is generated in the plastid by hydrolysis of ATP produced in mitochondria (Fig 1d,e and Fig. 2c). Conversely, in the light, respiration increases linearly with photosynthesis (Fig. 2b), and vice versa (Fig. 2d). This tight energetic coupling is likely instrumental for adjusting ...
Photosystems I and II convert solar energy into the chemical energy that powers life. Chlorophyll a photochemistry, using red light (680 to 700 nm), is near universal and is considered to define the energy "red limit" of oxygenic photosynthesis. We present biophysical studies on the photosystems from a cyanobacterium grown in far-red light (750 nm). The few long-wavelength chlorophylls present are well resolved from each other and from the majority pigment, chlorophyll a. Charge separation in photosystem I and II uses chlorophyll f at 745 nm and chlorophyll f (or d) at 727 nm, respectively. Each photosystem has a few even longer-wavelength chlorophylls f that collect light and pass excitation energy uphill to the photochemically active pigments. These photosystems function beyond the red limit using far-red pigments in only a few key positions.
All photosynthetic reaction centers share a common structural theme. Two related, integral membrane polypeptides sequester electron transfer cofactors into two quasi-symmetrical branches, each of which incorporates a quinone. In type II reaction centers [photosystem (PS) II and proteobacterial reaction centers], electron transfer proceeds down only one of the branches, and the mobile quinone on the other branch is used as a terminal acceptor. PS I uses iron-sulfur clusters as terminal acceptors, and the quinone serves only as an intermediary in electron transfer. Much effort has been devoted to understanding the unidirectionality of electron transport in type II reaction centers, and it was widely thought that PS I would share this feature. We have tested this idea by examining in vivo kinetics of electron transfer from the quinone in mutant PS I reaction centers. This transfer is associated with two kinetic components, and we show that mutation of a residue near the quinone in one branch specifically affects the faster component, while the corresponding mutation in the other branch specifically affects the slower component. We conclude that both electron transfer branches in PS I are active.
Abstract— The amount of oxygen evolved by Chlorella cells or by isolated chloroplasts has been measured after illumination by short saturating flashes. In all conditions, the amount of oxygen evolved by one flash is proportional to the fraction of the photochemical centers susceptible to produce oxygen. If dark adapted algae or chloroplasts are illuminated by a sene of flashes, no oxygen is produced by the first flash. This phenomenon is related to the activation process. If yn is the amount of oxygen evolved by the nth flash of the sequence, it appears that the sene yn shows large oscillations with a period 4. These oscillations are completely damped after 4–6 periods and the amount of oxygen evolved by a flash reaches a stationary value. For any value of n. the quantities yn and yn+2 are linked by a recurrent relation which is the same for Chlorella cells and spinach chloroplasts. No relation can be found between the terms yn and y(n+1). The mathematical properties of the series yn can be understood if one admits that a two memory process is involved in the photochemical reaction. The results have been interpreted in terms of a new model of the System II photochemical centers. The main characteristics of this model are: (1) Each photochemical center includes two electron donors (Z) and one electron acceptor (Q). (2) The formation of one atom of oxygen requires a two quantum process corresponding to the transfer of two electrons from the same electron donor (first memory). (3) The photochemical center acts as a switch which connects alternately each donor to the acceptor (second memory). The switch process occurs after each photoact with an efficiency of about 85 per cent. Other arguments in favor of this model are obtained from studies of the rate of oxygen production at the onset of a weak illumination.
Cyclic electron flow is increasingly recognized as being essential in plant growth, generating a pH gradient across thylakoid membrane (ΔpH) that contributes to ATP synthesis and triggers the protective process of nonphotochemical quenching (NPQ) under stress conditions. Here, we report experiments demonstrating the importance of that ΔpH in protecting plants from stress and relating to the regulation of cyclic relative to linear flow. In leaves infiltrated with low concentrations of nigericin, which dissipates the ΔpH without significantly affecting the potential gradient, thereby maintaining ATP synthesis, the extent of NPQ was markedly lower, reflecting the lower ΔpH. At the same time, the photosystem (PS) I primary donor P700 was largely reduced in the light, in contrast to control conditions where increasing light progressively oxidized P700, due to down-regulation of the cytochrome bf complex. Illumination of nigericin-infiltrated leaves resulted in photoinhibition of PSII but also, more markedly, of PSI. Plants lacking ferredoxin (Fd) NADP oxidoreductase (FNR) or the polypeptide proton gradient regulation 5 (PGR5) also show reduction of P700 in the light and increased sensitivity to PSI photoinhibition, demonstrating that the regulation of the cytochrome bf complex (cyt bf) is essential for protection of PSI from light stress. The formation of a ΔpH is concluded to be essential to that regulation, with cyclic electron flow playing a vital, previously poorly appreciated role in this protective process. Examination of cyclic electron flow in plants with a reduced content of FNR shows that these antisense plants are less able to maintain a steady rate of this pathway. This reduction is suggested to reflect a change in the distribution of FNR from cyclic to linear flow, likely reflecting the formation or disassembly of FNR–cytochrome bf complex.
Chloroplasts of land plants characteristically contain grana, cylindrical stacks of thylakoid membranes. A granum consists of a core of appressed membranes, two stroma-exposed end membranes, and margins, which connect pairs of grana membranes at their lumenal sides. Multiple forces contribute to grana stacking, but it is not known how the extreme curvature at margins is generated and maintained. We report the identification of the CURVATURE THYLAKOID1 (CURT1) protein family, conserved in plants and cyanobacteria. The four Arabidopsis thaliana CURT1 proteins (CURT1A, B, C, and D) oligomerize and are highly enriched at grana margins. Grana architecture is correlated with the CURT1 protein level, ranging from flat lobe-like thylakoids with considerably fewer grana margins in plants without CURT1 proteins to an increased number of membrane layers (and margins) in grana at the expense of grana diameter in overexpressors of CURT1A. The endogenous CURT1 protein in the cyanobacterium Synechocystis sp PCC6803 can be partially replaced by its Arabidopsis counterpart, indicating that the function of CURT1 proteins is evolutionary conserved. In vitro, Arabidopsis CURT1A proteins oligomerize and induce tubulation of liposomes, implying that CURT1 proteins suffice to induce membrane curvature. We therefore propose that CURT1 proteins modify thylakoid architecture by inducing membrane curvature at grana margins.
The turnover of linear and cyclic electron flows has been determined in fragments of dark-adapted spinach leaf by measuring the kinetics of fluorescence yield and of the transmembrane electrical potential changes under saturating illumination. When Photosystem (PS) II is inhibited, a cyclic electron flow around PSI operates transiently at a rate close to the maximum turnover of photosynthesis. When PSII is active, the cyclic flow operates with a similar rate during the first seconds of illumination. The high efficiency of the cyclic pathway implies that the cyclic and the linear transfer chains are structurally isolated one from the other. We propose that the cyclic pathway operates within a supercomplex including one PSI, one cytochrome bf complex, one plastocyanin, and one ferredoxin. The cyclic process induces the synthesis of ATP needed for the activation of the Benson-Calvin cycle. A fraction of PSI (ϳ50%), not included in the supercomplexes, participates in the linear pathway. The illumination would induce a dissociation of the supercomplexes that progressively increases the fraction of PSI involved in the linear pathway.I t is widely assumed that the photosynthetic process in algae or plants operates according to two nonmutually exclusive modes: linear and cyclic electron flows. In the linear mode, electrons are transferred from water to the NADP via the three major complexes of the photosynthetic chain, Photosystem (PS) II, cytochrome b 6 f (cyt bf), and PSI (1). Little is known, however, about the mechanism of the cyclic process that was first characterized by Arnon (2) in broken chloroplasts. In unicellular algae, a cyclic electron flow operates in anaerobic conditions (3, 4). In higher plants, the occurrence of a cyclic flow in vivo is a subject of controversy (reviewed in refs. 5 and 6). On the basis of a parallel measurement of PSI and PSII yield, Harbinson and Foyer (7) concluded that a cyclic process operates at a significant rate during the induction period but not in steady-state conditions. Heber et al. (8) reported that a decrease of CO 2 concentration stimulates the cyclic flow. At variance, Klughammer and Schreiber (9) conclude that no significant cyclic flow contributes to PSI turnover during the induction period or in the absence of CO 2 . It is generally reported that in steady-state conditions in the presence of CO 2 , the linear pathway is largely favored with respect to the cyclic flow. Bendall and Manasse (6) concluded that the rate of the cyclic process is no more than 3% of that of the linear pathway.It is agreed that both PSI and cyt bf complexes are involved in the cyclic flow. Yet, the mechanism of electron transfer between the PSI acceptor side and the cyt bf complex is not clearly identified. It has been proposed that reduced ferredoxin (Fd) or NADP may transfer electrons to plastoquinone (PQ) by way of a membrane-bound Fd PQ-reductase or NADP dehydrogenase (NDH). Plastoquinol (PQH 2 ) is then reoxidized at the PQH 2 -oxidizing site Q o of the cyt bf complex. This hypothesis i...
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