Abstract:In photosynthetic systems of oxygenic type, plastoquinone (PQ) molecules are reduced by photosystem II (PSII). The turnover of PQ determines the rate of PSII operation. PQ molecules are present in surplus with respect to PSII. In this work, using the pulse amplitude modulation‐fluorometry technique, we quantified photo‐reducible PQ pools in chloroplasts of two contrasting ecotypes of Tradescantia, acclimated either to low light (~ 100 μmol photons·m−2·s−1, LL) or to high light (~ 1000 μmol photons·m−2·s−1, HL)… Show more
“…In the case of the previously described mechanism, when reduced Q B is proposed to leave and be replaced by another oxidized Q B , this step would limit the electron transfer in the PSII part of all the electron-transport chain, and newly arrived electrons will be stuck on the Q A − stage, increasing the probability of forming radicals and damaging PSII subunits. The observation that the plastoquinone pool of Nannochloropsis oceanica was not completely reduced during the bright light pulses [36], as well as in the plants [37], is in line with this study's proposal for the mechanism of photoprotection in C. ohadii.…”
Section: Resultssupporting
confidence: 90%
“…trons will be stuck on the QA stage, increasing the probability of forming radicals and damaging PSII subunits. The observation that the plastoquinone pool of Nannochloropsis oceanica was not completely reduced during the bright light pulses [36], as well as in the plants [37], is in line with this study's proposal for the mechanism of photoprotection in C. ohadii.…”
Green alga Chlorella ohadii is known for its ability to carry out photosynthesis under harsh conditions. Using cryogenic electron microscopy (cryoEM), we obtained a high-resolution structure of PSII at 2.72 Å. This structure revealed 64 subunits, which encompassed 386 chlorophylls, 86 carotenoids, four plastoquinones, and several structural lipids. At the luminal side of PSII, a unique subunit arrangement was observed to protect the oxygen-evolving complex. This arrangement involved PsbO (OEE1), PsbP (OEE2), PsbB, and PsbU (a homolog of plant OEE3). PsbU interacted with PsbO, PsbC, and PsbP, thereby stabilizing the shield of the oxygen-evolving complex. Significant changes were also observed at the stromal electron acceptor side. PsbY, identified as a transmembrane helix, was situated alongside PsbF and PsbE, which enclosed cytochrome b559. Supported by the adjacent C-terminal helix of Psb10, these four transmembrane helices formed a bundle that shielded cytochrome b559 from the surrounding solvent. Moreover, the bulk of Psb10 formed a protective cap, which safeguarded the quinone site and likely contributed to the stacking of PSII complexes. Based on our findings, we propose a protective mechanism that prevents QB (plastoquinone B) from becoming fully reduced. This mechanism offers insights into the regulation of electron transfer within PSII.
“…In the case of the previously described mechanism, when reduced Q B is proposed to leave and be replaced by another oxidized Q B , this step would limit the electron transfer in the PSII part of all the electron-transport chain, and newly arrived electrons will be stuck on the Q A − stage, increasing the probability of forming radicals and damaging PSII subunits. The observation that the plastoquinone pool of Nannochloropsis oceanica was not completely reduced during the bright light pulses [36], as well as in the plants [37], is in line with this study's proposal for the mechanism of photoprotection in C. ohadii.…”
Section: Resultssupporting
confidence: 90%
“…trons will be stuck on the QA stage, increasing the probability of forming radicals and damaging PSII subunits. The observation that the plastoquinone pool of Nannochloropsis oceanica was not completely reduced during the bright light pulses [36], as well as in the plants [37], is in line with this study's proposal for the mechanism of photoprotection in C. ohadii.…”
Green alga Chlorella ohadii is known for its ability to carry out photosynthesis under harsh conditions. Using cryogenic electron microscopy (cryoEM), we obtained a high-resolution structure of PSII at 2.72 Å. This structure revealed 64 subunits, which encompassed 386 chlorophylls, 86 carotenoids, four plastoquinones, and several structural lipids. At the luminal side of PSII, a unique subunit arrangement was observed to protect the oxygen-evolving complex. This arrangement involved PsbO (OEE1), PsbP (OEE2), PsbB, and PsbU (a homolog of plant OEE3). PsbU interacted with PsbO, PsbC, and PsbP, thereby stabilizing the shield of the oxygen-evolving complex. Significant changes were also observed at the stromal electron acceptor side. PsbY, identified as a transmembrane helix, was situated alongside PsbF and PsbE, which enclosed cytochrome b559. Supported by the adjacent C-terminal helix of Psb10, these four transmembrane helices formed a bundle that shielded cytochrome b559 from the surrounding solvent. Moreover, the bulk of Psb10 formed a protective cap, which safeguarded the quinone site and likely contributed to the stacking of PSII complexes. Based on our findings, we propose a protective mechanism that prevents QB (plastoquinone B) from becoming fully reduced. This mechanism offers insights into the regulation of electron transfer within PSII.
“…There is direct experimental evidence, not just correlative evidence, supporting the assumption about how the state of the PQ pool and its saturation affect photosynthetic dynamics (Joliot and Joliot, 1984a, 1984bJoliot, 2003;Rokke et al, 2017;Suslichenko and Tikhonov, 2019). There is comparable additional evidence for the influence of the PQ pool on photosynthetic efficiency from investigations of direct hydrogen production (rather than biomass generation) from algae (Greenbaum, 1979) where the same rate-limiting steps in PS II dominate photosynthetic yield.…”
Section: Pq Pool and Pulsed-light Operationmentioning
We present experimental results demonstrating that, relative to continuous illumination, an increase of a factor of 3-10 in the photon efficiency of algal photosynthesis is attainable via the judicious application of pulsed light for light intensities of practical interest (e.g., average-to-peak solar irradiance). We also propose a simple model that can account for all the measurements. The model (1) reflects the essential rate-limiting elements in bioproductivity, (2) incorporates the impact of photon arrival-time statistics, and (3) accounts for how the enhancement in photon efficiency depends on the timescales of light pulsing and photon flux density. The key is avoiding ''clogging'' of the photosynthetic pathway by properly timing the light-dark cycles experienced by algal cells. We show how this can be realized with pulsed light sources, or by producing pulsed-light effects from continuous illumination via turbulent mixing in dense algal cultures in thin photobioreactors.
“…In normal growth conditions, up to 50% of the PQ-9 pool in plant leaves is located in the thylakoid membranes where it participates in electron transport from PSII to the cytochrome b6/f. The number of PQ-9 molecules per PSII has been estimated to be around 10-15 [27,29,30] although some lower values were reported [31]. The total PQ-9 concentration in plants can vary considerably with the environmental conditions, but the amount of photochemically active PQ-9 in the thylakoid membrane seems to be rather constant [27], possibly representing an optimal value for photosynthesis.…”
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