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1.
Photosynth Res ; 141(2): 165-179, 2019 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-30701483

RESUMO

In the present study, we have investigated the effect of hydroxyectoine (Ect-OH), a heterocyclic amino acid, on oxygen evolution in photosystem II (PS II) membrane fragments and on photoinhibition of Mn-depleted PS II (apo-WOC-PS II) preparations. The degree of photoinhibition of apo-WOC-PS II preparations was estimated by the loss of the capability of exogenous electron donor (sodium ascorbate) to restore the amplitude of light-induced changes of chlorophyll fluorescence yield (∆F). It was found that Ect-OH (i) stimulates the oxygen-evolving activity of PS II, (ii) accelerates the electron transfer from exogenous electron donors (K4[Fe(CN)6], DPC, TMPD, Fe2+, and Mn2+) to the reaction center of apo-WOC-PS II, (iii) enhances the protective effect of exogenous electron donors against donor-side photoinhibition of apo-WOC-PS II preparations. It is assumed that Ect-OH can serve as an artificial electron donor for apo-WOC-PS II, which does not directly interact with either the donor or acceptor side of the reaction center. We suggest that the protein conformation in the presence of Ect-OH, which affects the extent of hydration, becomes favorable for accepting electrons from exogenous donors. To our knowledge, this is the first study dealing with redox activity of Ect-OH towards photosynthetic pigment-protein complexes.


Assuntos
Diamino Aminoácidos/farmacologia , Transporte de Elétrons/efeitos dos fármacos , Manganês/metabolismo , Oxigênio/metabolismo , Complexo de Proteína do Fotossistema II/metabolismo , Spinacia oleracea/fisiologia , Elétrons , Oxirredução/efeitos dos fármacos , Folhas de Planta/fisiologia , Água/metabolismo
2.
Photosynth Res ; 133(1-3): 129-138, 2017 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-28349346

RESUMO

Earlier the catalase-insensitive formation of organic hydroperoxides (via the interaction of organic radicals produced due to redox activity of P680+· (or TyrZ·) with molecular oxygen) has been found in Mn-depleted PS2 preparations (apo-WOC-PS2) by Khorobrykh et al. (Biochemistry 50:10658-10665, 2011). The present work describes a second pathway of the photoproduction of organic peroxides on the donor side of PS2. It was shown that illumination of CaCl2-treated PS2 membranes (deprived of the PS2 extrinsic proteins without removal of the Mn-containing water-oxidizing complex) (CaCl2-PS2) led to the photoproduction of highly lipophilic organic hydroperoxides (LP-OOH) (in amount corresponding to 1.5 LP-OOH per one reaction center of PS2) which significantly increased upon the addition of exogenous electron acceptor potassium ferricyanide (to 4.2 LP-OOH per one reaction center). Addition of catalase (200 U/ml) before illumination inhibited ferricyanide-induced photoproduction of hydroperoxides while no effect was obtained by adding catalase after illumination or by adding inactivated catalase before illumination. The hydroperoxide photoproduction was inhibited by the addition of exogenous electron donor for PS2, diphenylcarbazide or diuron (inhibitor of the electron transfer in PS2). The addition of exogenous hydrogen peroxide to the CaCl2-PS2 led to the production of highly lipophilic organic hydroperoxides in the dark (3.2 LP-OOH per one reaction center). We suggest that the photoproduction of highly lipophilic organic hydroperoxides in CaCl2-PS2 preparations occurs via redox activity of H2O2 produced on the donor side of PS2.


Assuntos
Cloroplastos/metabolismo , Peróxido de Hidrogênio/metabolismo , Membranas Intracelulares/metabolismo , Luz , Complexo de Proteína do Fotossistema II/metabolismo , Spinacia oleracea/metabolismo , Catalase/metabolismo , Cloroplastos/efeitos da radiação , Escuridão , Fluorescência , Membranas Intracelulares/efeitos da radiação , Cinética , Lipídeos/química , Oxirredução , Spinacia oleracea/efeitos da radiação
3.
Biochemistry (Mosc) ; 80(1): 61-6, 2015 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-25754040

RESUMO

The pigment-protein complex of photosystem 2 (PS 2) catalyzes the light-driven oxidation of water molecule and the reduction of plastoquinone. In this work, we studied the effect of the disaccharide trehalose, which is unique in its physicochemical properties, on isolated PS 2 complex. It was found that trehalose significantly stimulated the steady-state rate of oxygen evolution. The study of single flash-induced fluorescence decay kinetics demonstrated that trehalose did not affect the rate of QA(-) oxidation, although it led to an increase in the relative fractions of PS 2 reaction centers capable of QA(-) oxidation. Trehalose also prevented PS 2 complexes from being inactivated on prolonged storage. We propose that in the presence of trehalose, which affects the extent of hydration, the protein can preferentially exist in a more optimal conformation for effective functioning.


Assuntos
Complexo de Proteína do Fotossistema II/metabolismo , Trealose/farmacologia , Transporte de Elétrons/efeitos dos fármacos , Oxirredução/efeitos dos fármacos , Complexo de Proteína do Fotossistema II/efeitos dos fármacos , Plastoquinona/química , Plastoquinona/metabolismo , Substâncias Protetoras/farmacologia , Spinacia oleracea/metabolismo
4.
Biochemistry (Mosc) ; 79(3): 205-12, 2014 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-24821446

RESUMO

Photosystem II (PSII) is a pigment-protein complex of thylakoid membrane of higher plants, algae, and cyanobacteria where light energy is used for oxidation of water and reduction of plastoquinone. Light-dependent reactions (generation of excited states of pigments, electron transfer, water oxidation) taking place in PSII can lead to the formation of reactive oxygen species. In this review attention is focused on the problem of interaction of molecular oxygen with the donor site of PSII, where after the removal of manganese from the water-oxidizing complex illumination induces formation of long-lived states (P680(+•) and TyrZ(•)) capable of oxidizing surrounding organic molecules to form radicals.


Assuntos
Oxigênio/química , Complexo de Proteína do Fotossistema II/química , Água/química , Transporte de Elétrons , Peróxido de Hidrogênio/química , Peróxido de Hidrogênio/metabolismo , Manganês/química , Oxirredução , Complexo de Proteína do Fotossistema II/metabolismo , Espécies Reativas de Oxigênio/química , Espécies Reativas de Oxigênio/metabolismo
5.
Photosynth Res ; 117(1-3): 367-74, 2013 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-23756831

RESUMO

It has been shown that removal of manganese from the water-oxidizing complex (WOC) of photosystem II (PSII) leads to flash-induced oxygen consumption (FIOC) which is activated by low concentration of Mn(2+) (Yanykin et al., Biochim Biophys Acta 1797:516-523, 2010). In the present work, we examined the effect of transition and non-transition divalent metal ions on FIOC in Mn-depleted PSII (apo-WOC-PSII) preparations. It was shown that only Mn(2+) ions are able to activate FIOC while other transition metal ions (Fe(2+), V(2+) and Cr(2+)) capable of electron donation to the apo-WOC-PSII suppressed the photoconsumption of O2. Co(2+) ions with a high redox potential (E (0) for Co(2+)/Co(3+) is 1.8 V) showed no effect. Non-transition metal ions Ca(2+) by Mg(2+) did not stimulate FIOC. However, Ca(2+) (in contrast to Mg(2+)) showed an additional activation effect in the presence of exogenic Mn(2+). The Ca(2+) effect depended on the concentration of both Mn(2+) and Ca(2+). The Ca effect was only observed when: (1) the activation of FIOC induced by Mn(2+) did not reach its maximum, (2) the concentration of Ca(2+) did not exceed 40 µM; at higher concentrations Ca(2+) inhibited the Mn(2+)-activated O2 photoconsumption. Replacement of Ca(2+) by Mg(2+) led to a suppression of Mn(2+)-activated O2 photoconsumption; while, addition of Ca(2+) resulted in elimination of the Mg(2+) inhibitory effect and activation of FIOC. Thus, only Mn(2+) and Ca(2+) (which are constituents of the WOC) have specific effects of activation of FIOC in apo-WOC-PSII preparations. Possible reactions involving Mn(2+) and Ca(2+) which could lead to the activation of FIOC in the apo-WOC-PSII are discussed.


Assuntos
Cálcio/farmacologia , Cloroplastos/metabolismo , Membranas Intracelulares/metabolismo , Manganês/farmacologia , Consumo de Oxigênio , Complexo de Proteína do Fotossistema II/metabolismo , Spinacia oleracea/metabolismo , Cátions Bivalentes/farmacologia , Cloroplastos/efeitos dos fármacos , Membranas Intracelulares/efeitos dos fármacos , Íons , Cinética , Consumo de Oxigênio/efeitos dos fármacos , Spinacia oleracea/efeitos dos fármacos
6.
Biochim Biophys Acta Bioenerg ; 1861(11): 148260, 2020 11 01.
Artigo em Inglês | MEDLINE | ID: mdl-32679044

RESUMO

A comparative analysis of functional characteristics of the grapevine leaf photosynthetic apparatus (LPA) and corticular photosynthetic apparatus (CPA) in chlorenchyma tissues of first-year lignified vine was performed. Obtained results demonstrate significant differences between the functional properties of the CPA and the LPA. CPA contains an increased proportion (about 2/3) of QB-non-reducing centers of photosystem II (PSII) that is confirmed by elevated O-J phase in fluorescence kinetics, high PSIIß content, and slower QA-• reoxidation. CPA and LPA use different strategies to utilize absorbed light energy and to protect itself against excessive light. CPA dissipates a significant proportion of absorbed light energy as heat (regulated and non-regulated dissipation), and only a smaller part of the excitation energy is used in the dark stages of photosynthesis. The rate constant of photoinhibition and fluorescence quenching due to photoinhibition in CPA is almost three times higher than in LPA, while high-energy state fluorescence quenching value is twice lower. The saturation of vine chlorenchyma tissue with water increases the CPA tolerance to photoinhibition and promotes the ability to restore the photosynthetic activity after photoinhibition. The electron microscopy analysis confirmed the presence of intact plastids in vine chlorenchyma tissue, the interior space of plastids is filled with large starch grains while bands of stacked thylakoid membranes are mainly localized on the periphery. Analyzes showed that corticular plastids are specialized organelles combining features of chloroplasts, amyloplasts and gerontoplasts. Distinct structural organization of photosynthetic membranes and microenvironment predetermine distinctive functional properties of CPA.


Assuntos
Clorofila/metabolismo , Cloroplastos/metabolismo , Fluorescência , Fotossíntese , Complexo de Proteína do Fotossistema II/metabolismo , Folhas de Planta/fisiologia , Vitis/fisiologia , Transporte de Elétrons , Luz
7.
J Photochem Photobiol B ; 163: 211-5, 2016 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-27588718

RESUMO

It has been shown earlier (Khorobrykh and Klimov, 2015) that molecular oxygen is directly involved in the general mechanism of the donor side photoinhibition of photosystem II (PSII) membranes. In the present work the effect of oxygen on photoassembly ("photoactivation") of the functionally active inorganic core of the water-oxidizing complex (WOC) in Mn-depleted PSII preparations (apo-WOC-PSII) in the presence of exogenous Mn(2+), Ca(2+) as well as ferricyanide was investigated. It was revealed that the efficiency of the photoassembly of the WOC was considerably increased upon removal of oxygen from the medium during photoactivation procedure using the enzymatic oxygen trap or argon flow. The lowering of O2 concentration from 250µM to 75µM, 10µM and near 0µM results in 29%, 71% and 92%, respectively, stimulation of the rate of O2 evolution measured after the photoactivation. The increase in the intensity of light used during the photoactivation was accompanied by a decrease of both the efficiency of photoassembly of the WOC and the stimulation effect of removal of O2 (that may be due to the enhancement of the processes leading to the photodamage to PSII). It is concluded that the enhancement in photoactivation of oxygen-evolving activity of apo-WOC-PSII induced by oxygen removal from the medium is due to the suppression of the donor side photoinhibition of PSII in which molecular oxygen can be involved.


Assuntos
Membrana Celular/metabolismo , Manganês , Complexo de Proteína do Fotossistema II/química , Complexo de Proteína do Fotossistema II/metabolismo , Água/metabolismo , Anaerobiose , Apoenzimas/química , Apoenzimas/metabolismo , Membrana Celular/efeitos da radiação , Oxirredução/efeitos da radiação , Spinacia oleracea/citologia
8.
J Photochem Photobiol B ; 164: 236-243, 2016 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-27693844

RESUMO

Recently, it has been shown that the addition of 1M trehalose leads to the increase of the rate of oxygen photoconsumption associated with activation of electron transport in the reaction center of photosystem 2 (PS2) in Mn-depleted PS2 membranes (apo-WOC-PS2) [37]. In the present work the effect of trehalose on photoinhibition of apo-WOC-PS2 preparations (which are characterized by a high sensitivity to the donor side photoinhibition of PS2) was investigated. The degree of photoinhibition was estimated by the loss of the capability of exogenous electron donor (sodium ascorbate) to reactivate the electron transport (measured by light-induced changes of chlorophyll fluorescence yield (∆F)) in apo-WOC-PS2. It was found that 1M trehalose enhanced the Mn2+-dependent suppression of photoinhibition of apo-WOC-PS2: in the presence of trehalose the addition of 0.2µM Mn2+ (corresponding to 2 Mn2+ per one reaction center) was sufficient for an almost complete suppression of the donor side photoinhibition of the complex. In the absence of trehalose it was necessary to add 100µM Mn2+ to achieve a similar result. The effect of trehalose was observed during photoinhibition of apo-WOC-PS2 at low (15µmolphotons-1m-2) and high (200µmolphotons-1m-2) light intensity. When Mn2+ was replaced by other PS2 electron donors (ferrocyanide, DPC) as well as by Ca2+ the protective effect of trehalose was not observed. It was also found that 1M trehalose decreased photoinhibition of apo-WOC-PS2 if the samples contained endogenous manganese (1-2 Mn ions per one RC was enough for the maximum protection effect). It is concluded that structural changes in PS2 caused by the addition of trehalose enhance the capability of photochemical reaction centers of apo-WOC-PS2 to accept electrons from manganese (both exogenous and endogenous), which in turn leads to a considerable suppression of the donor side photoinhibition of PS2.


Assuntos
Manganês/farmacologia , Complexo de Proteína do Fotossistema II/metabolismo , Trealose/farmacologia
9.
J Photochem Photobiol B ; 152(Pt B): 279-85, 2015 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-26386978

RESUMO

It is known that the removal of manganese from the water-oxidizing complex (WOC) of photosystem 2 (PS2) leads to activation of oxygen photoconsumption (OPC) [Khorobrykh et al., 2002; Yanykin et al., 2010] that is accompanied by the formation of organic hydroperoxides on the electron-donor side of PS2 [Khorobrykh et al., 2011]. In the present work the effect of trehalose on the OPC in Mn-depleted PS2 preparations (apo-WOC-PS2) was investigated. A more than two-fold increase of the OPC is revealed upon the addition of 1M trehalose. Drastic (30%-70%) inhibition of the OPC upon the addition of either electron acceptor or electron donor indicates that the trehalose-induced activation of the OPC occurs on both donor and acceptor sides of PS2. A two-fold increase in the rate of superoxide-anion radical photoproduction on the electron-acceptor side of PS2 was also shown. Applying the "variable" chlorophyll fluorescence (ΔF) it was shown that the addition of trehalose induces: (i) a significant increase in the ability of exogenous Mn(2+) to donate electrons to the reaction center of PS2, (ii) slowing down the photoaccumulation of the primary quinone electron acceptor of PS2 (QA(-)) under aerobic conditions, (iii) acceleration of the reoxidation of QA(-) by QB (and by QB(-)) as well as the replacement of QB(2-) by a fully oxidized plastoquinone, and (iv) restoration of the electron transfer between the quinone electron carriers in the so-called "closed reaction centers of PS2" (their content in the apo-WOC-PS2 is 41%). It is suggested that the trehalose-induced increase in efficiency of the O2 interaction with the electron-donor and electron-acceptor sides of apo-WOC-PS2 is due to structural changes leading to both a decrease in the proportion of the "closed PS2 reaction centers" and an increase in the electron transfer rate in PS2.


Assuntos
Luz , Manganês , Oxigênio/metabolismo , Complexo de Proteína do Fotossistema II/química , Complexo de Proteína do Fotossistema II/metabolismo , Tilacoides/metabolismo , Trealose/farmacologia , Clorofila/metabolismo , Relação Dose-Resposta a Droga , Transporte de Elétrons/efeitos dos fármacos , Transporte de Elétrons/efeitos da radiação , Spinacia oleracea/citologia , Tilacoides/efeitos dos fármacos , Tilacoides/efeitos da radiação , Água/metabolismo
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