Carotenoid‐induced quenching of the phycobilisome fluorescence in photosystem II‐deficient mutant of <i>Synechocystis</i> sp.

Rakhimberdieva, M. G.; Stadnichuk, Igor N.; Elanskaya, I.V.; Karapetyan, N. V.

doi:10.1016/j.febslet.2004.07.087

Cited by 145 publications

(111 citation statements)

References 27 publications

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“…By increasing the thermal dissipation of the absorbed energy, OCP decreases energy arriving at the photosynthetic reaction centers (Wilson et al, 2006). This photoprotective mechanism is activated by blue-green light but not by orange or red light, which are not absorbed by OCP (Rakhimberdieva et al, 2004;Wilson et al, 2006). OCP has an a-helical N-terminal domain (residues 15 to 165) and an a/b C-terminal domain (residues 190 to 317).…”

Section: Introductionmentioning

confidence: 99%

The Cyanobacterial Photoactive Orange Carotenoid Protein Is an Excellent Singlet Oxygen Quencher

et al. 2014

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Cyanobacteria have developed a photoprotective mechanism that decreases the energy arriving at the photosynthetic reaction centers under high-light conditions. The photoactive orange carotenoid protein (OCP) is essential in this mechanism as a light sensor and energy quencher. When OCP is photoactivated by strong blue-green light, it is able to dissipate excess energy as heat by interacting with phycobilisomes. As a consequence, charge separation and recombination leading to the formation of singlet oxygen diminishes. Here, we demonstrate that OCP has another essential role. We observed that OCP also protects Synechocystis cells from strong orange-red light, a condition in which OCP is not photoactivated. We first showed that this photoprotection is related to a decrease of singlet oxygen concentration due to OCP action. Then, we demonstrated that, in vitro, OCP is a very good singlet oxygen quencher. By contrast, another carotenoid protein having a high similarity with the N-terminal domain of OCP is not more efficient as a singlet oxygen quencher than a protein without carotenoid. Although OCP is a soluble protein, it is able to quench the singlet oxygen generated in the thylakoid membranes. Thus, OCP has dual and complementary photoprotective functions as an energy quencher and a singlet oxygen quencher.

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Section: Introductionmentioning

confidence: 99%

The Cyanobacterial Photoactive Orange Carotenoid Protein Is an Excellent Singlet Oxygen Quencher

et al. 2014

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“…In contrast, the mechanism of thermal energy dissipation in cyanobacteria, which plays a key role in global carbon cycling, remained elusive. Only within the last few years has a photoprotective mechanism associated with the soluble phycobilisome antenna of PSII in cyanobacteria been demonstrated (8)(9)(10)(11)(12)(13)(14). A specific soluble carotenoid protein, the orange carotenoid protein (OCP), plays an essential role in this process (9,10).…”

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confidence: 99%

A photoactive carotenoid protein acting as light intensity sensor

Wilson

Punginelli

Gall

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

321

431

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Intense sunlight is dangerous for photosynthetic organisms. Cyanobacteria, like plants, protect themselves from light-induced stress by dissipating excess absorbed energy as heat. Recently, it was discovered that a soluble orange carotenoid protein, the OCP, is essential for this photoprotective mechanism. Here we show that the OCP is also a member of the family of photoactive proteins; it is a unique example of a photoactive protein containing a carotenoid as the photoresponsive chromophore. Upon illumination with blue-green light, the OCP undergoes a reversible transformation from its dark stable orange form to a red ''active'' form. The red form is essential for the induction of the photoprotective mechanism. The illumination induces structural changes affecting both the carotenoid and the protein. Thus, the OCP is a photoactive protein that senses light intensity and triggers photoprotection.cyanobacteria ͉ nonphotochemical quenching ͉ photoprotection ͉ phycobilisome

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“…It has been recently shown that, in cyanobacteria, like in plants, there exists a photoprotective process that decreases the energy transfer between the antenna and the reaction centers by increasing thermal dissipation (8)(9)(10)(11)(12)(13). However, this mechanism is not triggered by a lowering of the luminal pH, as occurs in plants;…”

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confidence: 99%

Identification of a protein required for recovery of full antenna capacity in OCP-related photoprotective mechanism in cyanobacteria

Boulay

Wilson

D’Haene

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

131

110

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High light can be lethal for photosynthetic organisms. Similar to plants, most cyanobacteria protect themselves from high irradiance by increasing thermal dissipation of excess absorbed energy. The photoactive soluble orange carotenoid protein (OCP) is essential for the triggering of this photoprotective mechanism. Light induces structural changes in the carotenoid and the protein, leading to the formation of a red active form. Through targeted gene interruption we have now identified a protein that mediates the recovery of the full antenna capacity when irradiance decreases. In Synechocystis PCC 6803, this protein, which we called the fluorescence recovery protein (FRP), is encoded by the slr1964 gene. Homologues of this gene are present in all of the OCP-containing strains. The FRP is a 14-kDa protein, strongly attached to the membrane, which interacts with the active red form of the OCP. In vitro this interaction greatly accelerates the conversion of the red OCP form to the orange form. We propose that in vivo, FRP plays a key role in removing the red OCP from the phycobilisome and in the conversion of the free red OCP to the orange inactive form. The discovery of FRP and its characterization are essential elements in the understanding of the OCPrelated photoprotective mechanism in cyanobacteria.carotenoid | nonphotochemical quenching | phycobilisome | photoreceptor | Synechocystis B ecause too much light can be lethal for photosynthetic organisms, photoprotection against excess absorbed light energy is an essential and universal attribute of oxygenic photosynthetic organisms. Survival, productivity, and habitat preference are largely determined by development of photoprotective mechanisms. One of these mechanisms, which is induced by high irradiance, dissipates the excess harmful absorbed energy into heat at the levels of the antennae.In all photosynthetic organisms, the function of the light harvesting antenna is similar: to collect and concentrate light energy in the photochemical reaction centers in which light energy is converted into chemical energy. In plants and green algae, light is principally harvested by membrane-embedded complexes noncovalently binding chlorophyll and carotenoid molecules. These complexes show a large structural and functional flexibility. They are reversibly switched from a very efficient energy collecting state into a photoprotected state. This state allows the conversion of excess energy into heat, decreasing the energy arriving at the reaction centers under high light conditions (1-4). Cyanobacteria are oxygenic photosynthetic prokaryotes that play a key role in global carbon cycling. To harvest light. most cyanobacteria use a large, membrane-extrinsic complex called the phycobilisome (PB), which is composed of several types of chromophorylated phycobiliproteins and of linker peptides (for reviews, see refs. 5-7).It has been recently shown that, in cyanobacteria, like in plants, there exists a photoprotective process that decreases the energy transfer between the antenna and ...

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Carotenoid‐induced quenching of the phycobilisome fluorescence in photosystem II‐deficient mutant of Synechocystis sp.

Cited by 145 publications

References 27 publications

The Cyanobacterial Photoactive Orange Carotenoid Protein Is an Excellent Singlet Oxygen Quencher

The Cyanobacterial Photoactive Orange Carotenoid Protein Is an Excellent Singlet Oxygen Quencher

A photoactive carotenoid protein acting as light intensity sensor

Identification of a protein required for recovery of full antenna capacity in OCP-related photoprotective mechanism in cyanobacteria

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