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Anne Joliot

Publications and source records attributed to Anne Joliot.

8 recordsLinked to original sources

On the advantages of using green light to study fluorescence yield changes in leaves.

In photosynthetic chains, the kinetics of fluorescence yield depends on the photochemical rates at the level of both Photosystem I and II and thus on the absorption cross section of the photosynthetic units as well as on the coupling between light harvesting complexes and photosynthetic traps. A new set-up is described which, at variance with the commonly used set-ups, uses of a weakly absorbed light source (light-emitting diodes with maximum output at 520 nm) to excite the photosynthetic electron chain and probe the resulting fluorescence yield changes and their time course. This approach optimizes the homogeneity of the exciting light throughout the leaf and we show that this homogeneity narrows the distribution of the photochemical rates. Although the exciting light is weakly absorbed, the possibility to tune the intensity of the light emitting diodes allows one to reach photochemical rates ranging from 10(4) s(-1) to 0.25 s(-1) rendering experimentally accessible different functional regimes. The variations of the fluorescence yield induced by the photosynthetic activity are qualitatively and quantitatively discussed. When illuminating dark-adapted leaves by a weak light, the kinetics of fluorescence changes displays a pronounced plateau which precedes the fluorescence increase reflecting the full reduction of the plastoquinone pool. We ascribe this plateau to the time delay needed to reduce the photosystem I electron acceptors.

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Cyclic electron flow in C3 plants.

This paper summarized our present view on the mechanism of cyclic electron flow in C3 plants. We propose that cyclic and linear pathways are in competition for the reoxidation of the soluble primary PSI acceptor, Ferredoxin (Fd), that freely diffuses in the stromal compartment. In the linear mode, Fd binds ferredoxin-NADP-reductase and electrons are transferred to NADP+ and then to the Benson and Calvin cycle. In the cyclic mode, Fd binds a site localized on the stromal side of the cytochrome b6f complex and electrons are transferred to P700 via a mechanism derived from the Q-cycle. In dark-adapted leaves, the cyclic flow operates at maximum rate, owing to the partial inactivation of the Benson and Calvin cycle. For increasing time of illumination, the activation of the Benson and Calvin cycle, and thus, that of the linear flow, is associated with a subsequent decrease in the rate of the cyclic flow. Under steady-state conditions of illumination, the contribution of cyclic flow to PSI turnover increases as a function of the light intensity (from 0 to approximately 50% for weak to saturating light, respectively). Lack of CO2 is associated with an increase in the efficiency of the cyclic flow. ATP concentration could be one of the parameters that control the transition between linear and cyclic modes.

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Quantification of cyclic and linear flows in plants.

A method was developed to quantify the fraction of photosystem I (PSI) centers that operate according to the cyclic or linear mode, respectively. P(700) and plastocyanin oxidation were analyzed under a weak far-red excitation (approximately eight photons per s(-1) per PSI) that induces P(700) oxidation in approximately 20 s and approximately 3 s in dark-adapted and preilluminated leaves, respectively. This finding implies that, in dark-adapted leaves, most of the electrons formed on the stromal side of PSI are transferred back to PSI through an efficient cyclic chain, whereas in preilluminated leaves, electrons are transferred to NADP and then to the Benson-Calvin cycle. Preillumination thus induces a transition from the cyclic to the linear mode. A reverse transition occurs in the dark in a time that increases with the duration and intensity of preillumination. After a approximately 10-min illumination under strong light that activates the Benson-Calvin cycle, the transition from the linear to the cyclic mode is completed in >1 h (t(1/2) approximately 30 min). The fraction of PSI involved in the cyclic process in dark-adapted leaves can be close to 100%. An apparent equilibrium constant of approximately 4 between P(700) and plastocyanin was measured during the course of the far-red illumination. This value is much lower than that computed from the midpoint redox potential of the two carriers (approximately 30). These results are interpreted assuming that chloroplasts include isolated compartments defined on the basis of the structural organization of the photosynthetic chain proposed by Albertsson [Albertsson, P. A. (2001) Trends Plant Sci. 6, 349-354].

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Fast oxidation of the primary electron acceptor under anaerobic conditions requires the organization of the photosynthetic chain of Rhodobacter sphaeroides in supercomplexes.

The kinetics of reoxidation of the primary acceptor Q(a) has been followed by measuring the changes in the fluorescence yield induced by a series of saturating flashes in intact cells of Rhodobacter sphaeroides in anaerobic conditions. At 0 degrees C, about half of Q(a)(-) is reoxidized in about 200 ms while reoxidation of the remaining fraction is completed in several seconds to minutes. The fast phase is associated with the transfer of ubiquinone formed at site Q(o) of the cytochrome bc(1) complex while the slowest phase is associated with the diffusion of ubiquinone present in the membrane prior to the flash excitation. The biphasic kinetics of Q(a)(-) oxidation is interpreted assuming that the electron chain is organized in supercomplexes that associate two RCs and one cyt bc(1) complex, which allows a fast transfer of quinone formed at the level of cyt bc(1) complex to the RCs. In agreement with this model, the fast phase of Q(a)(-) reoxidation is inhibited by myxothiazol, a specific inhibitor of cyt bc(1). The PufX-deleted mutant displays only the slowest phase of Q(a)(-) oxidation; it is interpreted by the lack of supramolecular organization of the photosynthetic chain that leads to a larger average distance between cyt bc(1) and RCs.

Anaerobiosis↗

Cyclic electron flow under saturating excitation of dark-adapted Arabidopsis leaves.

The rate of cyclic electron flow measured in dark-adapted leaves under aerobic conditions submitted to a saturating illumination has been performed by the analysis of the transmembrane potential changes induced by a light to dark transfer. Using a new highly sensitive spectrophotometric technique, a rate of the cyclic flow of approximately 130 s(-1) has been measured in the presence or absence of 3-(3,4-dichloro-phenyl)-1,1-dimethylurea (DCMU). This value is approximately 1.5 times larger than that previously reported [Proc. Natl. Acad. Sci. U. S. A. 99 (2001) 10209]. We have characterized in the presence or absence of DCMU charge recombination process (t(1/2) approximately 60 micros) that involves P(700)(+) and very likely the reduced form of the iron sulfur acceptor F(X). This led to conclude that, under saturating illumination, the PSI centers involved in the cyclic pathway have most of the iron sulfur acceptors F(A) and F(B) reduced. In the proposed mechanism, electrons are transferred from a ferredoxin bound to a site localized on the stromal side of the cytochrome b(6)f complex to the Q(i) site. Two possible models of the organization of the membrane complexes are discussed, in which the cyclic and linear electron transfer chains are isolated one from the other.

Adaptation, Physiological↗

Excitation transfer between photosynthetic units: the 1964 experiment.

We review here the background and the experiments that led to the concept of excitation energy transfer among photosystem (PS) II units. On the basis of a kinetic analysis of oxygen evolution and chlorophyll a fluorescence yield, the authors showed, in 1964, that the PS II photochemical reaction involved in the formation of oxygen is not a first-order process. We concluded that excitation energy localized in a 'photosynthetic unit' including a reduced primary acceptor is transferred with a high probability to neighboring PS II units. Here, the beginnings and the original data of this topic are presented.

Journal Article↗

Knock-out of the genes coding for the Rieske protein and the ATP-synthase delta-subunit of Arabidopsis. Effects on photosynthesis, thylakoid protein composition, and nuclear chloroplast gene expression.

In Arabidopsis, the nuclear genes PetC and AtpD code for the Rieske protein of the cytochrome b(6)/f (cyt b(6)/f) complex and the delta-subunit of the chloroplast ATP synthase (cpATPase), respectively. Knock-out alleles for each of these loci have been identified. Greenhouse-grown petc-2 and atpd-1 mutants are seedling lethal, whereas heterotrophically propagated plants display a high-chlorophyll (Chl)-fluorescence phenotype, indicating that the products of PetC and AtpD are essential for photosynthesis. Additional effects of the mutations in axenic culture include altered leaf coloration and increased photosensitivity. Lack of the Rieske protein affects the stability of cyt b(6)/f and influences the level of other thylakoid proteins, particularly those of photosystem II. In petc-2, linear electron flow is blocked, leading to an altered redox state of both the primary quinone acceptor Q(A) in photosystem II and the reaction center Chl P700 in photosystem I. Absence of cpATPase-delta destabilizes the entire cpATPase complex, whereas residual accumulation of cyt b(6)/f and of the photosystems still allows linear electron flow. In atpd-1, the increase in non-photochemical quenching of Chl fluorescence and a higher de-epoxidation state of xanthophyll cycle pigments under low light is compatible with a slower dissipation of the transthylakoid proton gradient. Further and clear differences between the two mutations are evident when mRNA expression profiles of nucleus-encoded chloroplast proteins are considered, suggesting that the physiological states conditioned by the two mutations trigger different modes of plastid signaling and nuclear response.

Arabidopsis↗

Cyclic electron transfer in plant leaf.

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 ( approximately 50%), 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.

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