Electrochromism: a useful probe to study algal photosynthesis

Bailleul, Benjamin; Cardol, Pierre; Breyton, Cécile; Finazzi, Guido

doi:10.1007/s11120-010-9579-z

Cited by 195 publications

(171 citation statements)

References 64 publications

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“…1F). The electrochromic shift (ECS) signal reflects changes in the electric field across the thylakoid membrane, and the total relaxation of the ECS signal during a light-dark transition represents the light-induced proton motive force (pmf; Bailleul et al, 2010). Due to the absence of photosynthetic electron transport in darkness, the initial ECS decay upon switching off actinic light mainly reflects proton efflux through ATP synthase; therefore, the H + conductivity of ATP synthase can be estimated based on the kinetics of the initial ECS decay (Cruz et al, 2001).…”

Section: Phenotype Of the Bfa3 Mutantmentioning

confidence: 99%

BIOGENESIS FACTOR REQUIRED FOR ATP SYNTHASE 3 Facilitates Assembly of the Chloroplast ATP Synthase Complex

et al. 2016

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Thylakoid membrane-localized chloroplast ATP synthases use the proton motive force generated by photosynthetic electron transport to produce ATP from ADP. Although it is well known that the chloroplast ATP synthase is composed of more than 20 proteins with a 3 b 3 g 1 « 1 d 1 I 1 II 1 III 14 IV 1 stoichiometry, its biogenesis process is currently unclear. To unravel the molecular mechanisms underlying the biogenesis of chloroplast ATP synthase, we performed extensive screening for isolating ATP synthase mutants in Arabidopsis (Arabidopsis thaliana). In the recently identified bfa3 (biogenesis factors required for ATP synthase 3) mutant, the levels of chloroplast ATP synthase subunits were reduced to approximately 25% of wild-type levels. In vivo labeling analysis showed that assembly of the CF 1 component of chloroplast ATP synthase was less efficient in bfa3 than in the wild type, indicating that BFA3 is required for CF 1 assembly. BFA3 encodes a chloroplast stromal protein that is conserved in higher plants, green algae, and a few species of other eukaryotic algae, and specifically interacts with the CF 1 b subunit. The BFA3 binding site was mapped to a region in the catalytic site of CF 1 b. Several residues highly conserved in eukaryotic CF 1 b are crucial for the BFA3-CF 1 b interaction, suggesting a coevolutionary relationship between BFA3 and CF 1 b. BFA3 appears to function as a molecular chaperone that transiently associates with unassembled CF 1 b at its catalytic site and facilitates subsequent association with CF 1 a during assembly of the CF 1 subcomplex of chloroplast ATP synthase.

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Section: Phenotype Of the Bfa3 Mutantmentioning

confidence: 99%

BIOGENESIS FACTOR REQUIRED FOR ATP SYNTHASE 3 Facilitates Assembly of the Chloroplast ATP Synthase Complex

et al. 2016

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“…The use of the ECS signal to study photosynthetic apparatus and a detailed description of the different application are reviewed in Bailleul et al (2010). The relaxation kinetics of the carotenoid electrochromic band shift was measured at 520 nm and corrected by subtracting the signal at 546 nm.…”

Section: Ecs Analysesmentioning

confidence: 99%

Induction of Photosynthetic Carbon Fixation in Anoxia Relies on Hydrogenase Activity and Proton-Gradient Regulation-Like1-Mediated Cyclic Electron Flow in Chlamydomonas reinhardtii

et al. 2015

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“…They modulate the electron transport rate via different feedback regulatory mechanisms. The transmembrane electric potential gradient is required for metabolite and protein transport across the membranes [1]. The ΔpH component (i.e., the acidification of the lumen) is involved, perhaps most prominently, in the photoprotective mechanisms of nonphotochemical quenching (NPQ) of the first singlet excited state of chlorophyll-a [2].…”

Section: Introductionmentioning

confidence: 99%

Low-pH induced reversible reorganizations of chloroplast thylakoid membranes — As revealed by small-angle neutron scattering

Ünnep¹,

Zsíros²,

Hörcsik³

et al. 2017

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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Energization of thylakoid membranes brings about the acidification of the lumenal aqueous phase, which activates important regulatory mechanisms. Earlier Jajoo and coworkers (2014 FEBS Lett. 588:970) have shown that low pH in isolated plant thylakoid membranes induces changes in the excitation energy distribution between the two photosystems. In order to elucidate the structural background of these changes, we used small-angle neutron scattering on thylakoid membranes exposed to low p 2 H (pD) and show that gradually lowering the p 2 H from 8.0 to 5.0 causes small but well discernible reversible diminishment of the periodic order and the lamellar repeat distance and an increased mosaicity -similar to the effects elicited by light-induced acidification of the lumen. Our data strongly suggest that thylakoids dynamically respond to the membrane energization and actively participate in different regulatory mechanisms. Keywords: chloroplast thylakoid membranes, lamellar repeat distance, low pH and p 2 H, smallangle neutron scattering (SANS) Highlights:1. Thylakoid membranes exposed to low p 2 H studied by small-angle neutron scattering 2. Acidification causes reversible shrinkage and diminished lamellar order 3. SANS changes induced by low pH resemble those due to light-induced lumenal acidification Abbreviations: p 2 H (pD), deuterium analogue of pH; NPQ, non-photochemical quenching; qE, the energy-dependent component of NPQ; ∆µ H + , transmembrane electrochemical potential gradient; PSI, photosystem I; PSII, photosystem II; LET, linear electron transport; CD, circular dichroism; SANS, small-angle neutron scattering; q, scattering vector; I, intensity; q*, center position of the Bragg peak; RD, repeat distance; φ, azimuthal angle; I(φ), angular dependency of the scattering intensity; FWHM, full width at half maximum 3

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Electrochromism: a useful probe to study algal photosynthesis

Cited by 195 publications

References 64 publications

BIOGENESIS FACTOR REQUIRED FOR ATP SYNTHASE 3 Facilitates Assembly of the Chloroplast ATP Synthase Complex

BIOGENESIS FACTOR REQUIRED FOR ATP SYNTHASE 3 Facilitates Assembly of the Chloroplast ATP Synthase Complex

Induction of Photosynthetic Carbon Fixation in Anoxia Relies on Hydrogenase Activity and Proton-Gradient Regulation-Like1-Mediated Cyclic Electron Flow in Chlamydomonas reinhardtii

Low-pH induced reversible reorganizations of chloroplast thylakoid membranes — As revealed by small-angle neutron scattering

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