RESUMEN
The natural oscillations of the electromagnetic field in a particle made from left-handed metamaterial, where both permittivity and permeability are negative, are considered. Based on the exact solution of the sourceless Maxwell equations, it is shown that due to the opposite directions of the phase and group velocities in the metamaterial, natural oscillations in such particles decay exponentially at infinity, that is, these natural oscillations can be considered as trapped modes with a finite energy. The manifestation of such modes in experiments with Bessel beams is also discussed.
RESUMEN
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.
Asunto(s)
Cloroplastos/metabolismo , Peróxido de Hidrógeno/metabolismo , Membranas Intracelulares/metabolismo , Luz , Complejo de Proteína del Fotosistema II/metabolismo , Spinacia oleracea/metabolismo , Catalasa/metabolismo , Cloroplastos/efectos de la radiación , Oscuridad , Fluorescencia , Membranas Intracelulares/efectos de la radiación , Cinética , Lípidos/química , Oxidación-Reducción , Spinacia oleracea/efectos de la radiaciónRESUMEN
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.
Asunto(s)
Manganeso/farmacología , Complejo de Proteína del Fotosistema II/metabolismo , Trehalosa/farmacologíaRESUMEN
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.
Asunto(s)
Membrana Celular/metabolismo , Manganeso , Complejo de Proteína del Fotosistema II/química , Complejo de Proteína del Fotosistema II/metabolismo , Agua/metabolismo , Anaerobiosis , Apoenzimas/química , Apoenzimas/metabolismo , Membrana Celular/efectos de la radiación , Oxidación-Reducción/efectos de la radiación , Spinacia oleracea/citologíaRESUMEN
Two-dimensional lattices of chiral nanoholes in a plasmonic film with lattice constants being slightly larger than light wavelength are proposed for effective control of polarization and spatial properties of light beams. Effective polarization conversion and strong circular dichroism in non-zero diffraction orders in these chiral metafilms are demonstrated by electromagnetic simulations. These interesting effects are found to result from interplay between radiation pattern of single chiral nanohole and diffraction pattern of the planar lattice, and can be manipulated by varying wavelength and polarization of incoming light as well as period of metastructure and refractive indexes of substrate and overlayer. Therefore, this work offers a novel paradigm for developing planar chiral metafilm-based optical devices with controllable polarization state, spatial orientation and intensity of outgoing light.
RESUMEN
The photosynthetic water oxidation in photosystem II (PS II) takes place in a special water-oxidizing complex (WOC) that consists of a catalytic center, Mn4CaO5 cluster, and also includes a group of extrinsic proteins needed for its stability. The most important of these is PsbO, which binds to the donor side of PS II near the Mn cluster and is directly involved in the regulation of its stability and activity. However, the molecular mechanism of PsbO involvement in photosynthetic water oxidation remains unclear. One of the main approaches to solving this problem is site-directed mutagenesis. Until recently, the effect of mutations in PsbO in vivo has been studied only in cyanobacteria (prokaryotes). In eukaryotic organisms, such studies (site-directed mutagenesis of PsbO) have not been carried out, though it is known that the role of PsbO protein in plants and cyanobacteria may be different. In this review, we consider the possibility of using for this purpose the unicellular green alga Chlamydomonas reinhardtii, a eukaryotic organism with a set of extrinsic proteins of the WOC similar to that of the higher plants. However, in contrast to higher plants, the ΔpsbO mutant of C. reinhardtii is viable. Another reason to use this alga is that the ΔpsbO strain of C. reinhardtii grown in the dark (heterotrophically) is able to build the minimal photochemically active complex of PS II, allowing investigation of the role of individual amino acid substitutions in PsbO in vivo without damaging PS II due to photoinactivation.
Asunto(s)
Chlamydomonas reinhardtii/genética , Chlamydomonas reinhardtii/metabolismo , Complejo de Proteína del Fotosistema II/genética , Complejo de Proteína del Fotosistema II/metabolismo , Sustitución de Aminoácidos , Mutagénesis Sitio-Dirigida/métodos , MutaciónRESUMEN
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.
Asunto(s)
Luz , Manganeso , Oxígeno/metabolismo , Complejo de Proteína del Fotosistema II/química , Complejo de Proteína del Fotosistema II/metabolismo , Tilacoides/metabolismo , Trehalosa/farmacología , Clorofila/metabolismo , Relación Dosis-Respuesta a Droga , Transporte de Electrón/efectos de los fármacos , Transporte de Electrón/efectos de la radiación , Spinacia oleracea/citología , Tilacoides/efectos de los fármacos , Tilacoides/efectos de la radiación , Agua/metabolismoRESUMEN
It has been shown by Khorobrykh et al. (Biochemistry (Moscow) 67:683-688, 2002); Yanykin et al. (Biochim Biophys Acta 1797:516-523, 2010); Khorobrykh et al. (Biochemistry 50:10658-10665, 2011) that Mn-depleted photosystem II (PSII) membrane fragments are characterized by an enhanced oxygen photoconsumption on the donor side of PSII which is accompanied with hydroperoxide formation and it was suggested that the events are related to the oxidative photoinhibition of PSII. Experimental confirmation of this suggestion is presented in this work. The degree of photoinhibition was determined by the loss of the capability of exogenous electron donors (Mn(2+) or sodium ascorbate) to the reactivation of electron transport [measured by the light-induced changes of chlorophyll fluorescence yield (∆F)] in Mn-depleted PSII membranes. The transition from anaerobic conditions to aerobic ones significantly activated photoinhibition of Mn-depleted PSII membranes both in the absence and in the presence of exogenous electron acceptor, ferricyanide. The photoinhibition of Mn-depleted PSII membranes was suppressed upon the addition of exogenous electron donors (Mn(2+), diphenylcarbazide, and ferrocyanide). The addition of superoxide dismutase did not affect the photoinhibition of Mn-depleted PSII membranes. It is concluded that the interaction of molecular oxygen (rather than superoxide anion radical formed on the acceptor side of PSII) with the oxidized components of the donor side of PSII reflects the involvement of O2 in the donor-side photoinhibition of Mn-depleted PSII membranes.
Asunto(s)
Oxígeno/metabolismo , Complejo de Proteína del Fotosistema II/metabolismo , Hojas de la Planta/fisiología , Spinacia oleracea/fisiología , Transporte de Electrón , Luz , Manganeso/deficiencia , Oxidación-Reducción , Superóxidos/metabolismoRESUMEN
Eigenmodes of a chiral sphere placed in a dielectric medium were investigated in details. Excitation of these eigenmodes by a plane wave and a chiral molecule radiation was studied both analytically and numerically. It was found that decay rates of "right" and "left" enantiomers are different in the presence of the chiral sphere. Strong dependence of radiation pattern of the chiral molecule placed in the vicinity of the chiral sphere on chirality strength was also demonstrated. An interesting correlation between chirality of sphere and spatial spirality (helicity, vorticity ...) of the electromagnetic fields in the presence of chiral sphere was observed for the first time.
RESUMEN
Oxylipins are signaling molecules formed enzymatically or spontaneously from unsaturated fatty acids in all aerobic organisms. Oxylipins regulate growth, development, and responses to environmental stimuli of organisms. The oxylipin biosynthesis pathway in plants includes a few parallel branches named after first enzyme of the corresponding branch as allene oxide synthase, hydroperoxide lyase, divinyl ether synthase, peroxygenase, epoxy alcohol synthase, and others in which various biologically active metabolites are produced. Oxylipins can be formed non-enzymatically as a result of oxygenation of fatty acids by free radicals and reactive oxygen species. Spontaneously formed oxylipins are called phytoprostanes. The role of oxylipins in biotic stress responses has been described in many published works. The role of oxylipins in plant adaptation to abiotic stress conditions is less studied; there is also obvious lack of available data compilation and analysis in this area of research. In this work we analyze data on oxylipins functions in plant adaptation to abiotic stress conditions, such as wounding, suboptimal light and temperature, dehydration and osmotic stress, and effects of ozone and heavy metals. Modern research articles elucidating the molecular mechanisms of oxylipins action by the methods of biochemistry, molecular biology, and genetics are reviewed here. Data on the role of oxylipins in stress signal transduction, stress-inducible gene expression regulation, and interaction of these metabolites with other signal transduction pathways in cells are described. In this review the general oxylipin-mediated mechanisms that help plants to adjust to a broad spectrum of stress factors are considered, followed by analysis of more specific responses regulated by oxylipins only under certain stress conditions. New approaches to improvement of plant resistance to abiotic stresses based on the induction of oxylipin-mediated processes are discussed.
Asunto(s)
Adaptación Fisiológica , Ambiente , Oxilipinas/metabolismo , Plantas/metabolismo , Desecación , Luz , Plantas/efectos de los fármacos , Plantas/genética , Plantas/efectos de la radiación , Transducción de Señal , TemperaturaRESUMEN
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(+â¢) and TyrZ(â¢)) capable of oxidizing surrounding organic molecules to form radicals.
Asunto(s)
Oxígeno/química , Complejo de Proteína del Fotosistema II/química , Agua/química , Transporte de Electrón , Peróxido de Hidrógeno/química , Peróxido de Hidrógeno/metabolismo , Manganeso/química , Oxidación-Reducción , Complejo de Proteína del Fotosistema II/metabolismo , Especies Reactivas de Oxígeno/química , Especies Reactivas de Oxígeno/metabolismoRESUMEN
Influence of bicarbonate on the efficiency of the electron donation from Mn(2+) to P680(+) in isolated D1/D2/cytochrome b559 complex was investigated. All the experiments were carried out in a medium depleted of HCO3(-)/CO2. Kinetics of photoinduced absorbance changes (ΔA) at different wavelengths and decrease of chlorophyll fluorescence yield (-ΔF) related to photoaccumulation of reduced pheophytin, the intermediary electron acceptor of photosystem II (PSII), in the presence of Mn(2+) under anaerobic conditions were measured. Addition of bicarbonate (1 mM) increased the amplitude of these ΔA and -ΔF at least by a factor of 3. Measurements of the photoinduced ΔA, related to photooxidation of the primary electron donor of PSII, chlorophyll P680, were done in the presence of silicomolybdate as electron acceptor. These results show that the addition of 0.05 mM Mn(2+) alone or jointly with 1 mM bicarbonate induces a 20% and 70%-decrease of the magnitude of the ΔA at 680 nm. The effect of Mn(2+) (in the presence and absence of bicarbonate) was completely eliminated by the addition of 12 mM EDTA. All these bicarbonate effects were not observed if MgCl2 or formate were used instead of MnCl2 and bicarbonate, respectively. In the absence of Mn(2+), bicarbonate induced none of the mentioned above effects (increase of photoaccumulation of reduced pheophytin and decrease of photooxidation of P680). The presented data suggest that bicarbonate stimulates the electron donation from Mn(2+) to D1/D2/cyt b559 reaction center evidently due to formation of easily oxidizable Mn-bicarbonate complexes.
Asunto(s)
Bicarbonatos/química , Grupo Citocromo b/química , Manganeso/química , Complejo de Proteína del Fotosistema II/química , Transporte de Electrón , Electrones , Iones/química , Cinética , Complejo de Proteína del Fotosistema II/metabolismoRESUMEN
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.
Asunto(s)
Calcio/farmacología , Cloroplastos/metabolismo , Membranas Intracelulares/metabolismo , Manganeso/farmacología , Consumo de Oxígeno , Complejo de Proteína del Fotosistema II/metabolismo , Spinacia oleracea/metabolismo , Cationes Bivalentes/farmacología , Cloroplastos/efectos de los fármacos , Membranas Intracelulares/efectos de los fármacos , Iones , Cinética , Consumo de Oxígeno/efectos de los fármacos , Spinacia oleracea/efectos de los fármacosRESUMEN
Site-directed mutations were introduced into PsbO protein of photosystem 2 to study the role of two lysine residues, 223 and 226 (LGAKPPK), in the green alga Chlamydomonas reinhardtii. Lysines 223 and 226 homologous to His228 and His231 from cyanobacteria are located on the protein side facing the lumen and can participate in formation of a channel connecting the Mn cluster with the intrathylakoid space. The K223E and K226E mutants were generated on the basis of the ΔpsbO strain of C. reinhardtii with the substitution of glutamic acid for the lysine residues. The K226E mutation leads to a decrease in stability of the protein and development of the ΔpsbO phenotype (the absence of both photosynthetic activity of photosystem 2 and photoautotrophic growth), with substantially decreased PsbO content in the cells. In the case of K223E, the mutant strain accumulated the normal level of PsbO protein and was able to grow photoautotrophically and to evolve oxygen. However, the rate of oxygen evolution and the F(v)/F(m) ratio were reduced by 15-20% compared to the control. Also, the time of the dark decay of F(v) in the presence of DCMU in the cells of the K223E mutant was increased, indicating impairment in the water-oxidizing complex. In general, our study shows the importance of amino acids K223 and K226 located at the lumenal surface of PsbO protein for the activity of the water-oxidizing complex.
Asunto(s)
Chlamydomonas reinhardtii/metabolismo , Complejo de Proteína del Fotosistema II/metabolismo , Proteínas de Plantas/metabolismo , Secuencia de Aminoácidos , Sustitución de Aminoácidos , Datos de Secuencia Molecular , Mutagénesis Sitio-Dirigida , Oxidación-Reducción , Oxígeno/metabolismo , Proteínas de Plantas/química , Proteínas de Plantas/genética , Estabilidad Proteica , Estructura Cuaternaria de Proteína , Proteínas Recombinantes/química , Proteínas Recombinantes/genética , Proteínas Recombinantes/metabolismo , Alineación de Secuencia , Agua/químicaRESUMEN
It has been shown that thermoinactivation of the isolated D1/D2/cytochrome b(559) complex (RC) of photosystem 2 (PS-2) from pea under anaerobic conditions at 35°C in 20 mM Tris-HCl buffer (pH 7.2) depleted of HCO(3)(-), with 35 mM NaCl and 0.05% n-dodecyl-ß-maltoside, results in a decrease in photochemical activity measured by photoreduction of the PS-2 primary electron acceptor, pheophytin (by 50% after 3 min of heating), which is accompanied by aggregation of the D1 and D2 proteins. Bicarbonate, formate, and acetate anions added to the sample under these conditions differently influence the maintenance of photochemical activity: a 50% loss of photochemical activity occurs in 11.5 min of heating in the presence of bicarbonate and in 4 and 4.6 min in the presence of formate and acetate, respectively. The addition of bicarbonate completely prevents aggregation of the D1 and D2 proteins as opposed to formate and acetate (their presence has no effect on the aggregation during thermoinactivation). Since the isolated RCs have neither inorganic Mn/Ca-containing core of the water-oxidizing complex nor nonheme Fe(2+), it is supposed that bicarbonate specifically interacts with the hydrophilic domains of the D1 and D2 proteins, which prevents their structural modification that is a signal for aggregation of these proteins and the loss of photochemical activity.
Asunto(s)
Bicarbonatos/farmacología , Grupo Citocromo b/metabolismo , Complejo de Proteína del Fotosistema II/metabolismo , Acetatos/farmacología , Electrones , Formiatos/farmacología , Cinética , Oxidación-Reducción/efectos de los fármacos , Pisum sativum/metabolismo , Feofitinas/química , Feofitinas/metabolismo , Hojas de la Planta/metabolismo , TemperaturaRESUMEN
The change in the dark reduction rate of photooxidized reaction centers (RC) of type II from three anoxygenic bacteria (Rhodobacter sphaeroides R-26, Chromatium minutissimum, and Chloroflexus aurantiacus) having different redox potentials of the P(+)/P pair and availability of RC for exogenous electron donors was investigated upon the addition of Mn(2+) and HCO(3)(-). It was found that the dark reduction of P(870)(+) from Rb. sphaeroides R-26 is considerably accelerated upon the combined addition of 0.5 mM MnCl(2) and 30-75 mM NaHCO(3) (as a result of formation of "low-potential" complexes [Mn(HCO(3))(2)]), while MnCl(2) and NaHCO(3) added separately had no such effect. The effect is not observed either in RC from Cf. aurantiacus (probably due to the low oxidation potential of the primary electron donor, P(865), which results in thermodynamic difficulties of the redox interaction between P(865)(+) and Mn(2+)) or in RC from Ch. minutissimum (apparently due to the presence of the RC-bound cytochrome preventing the direct interaction between P(870)(+) and Mn(2+)). The absence of acceleration of the dark reduction of P(870)(+) in the RC of Rb. sphaeroides R-26 when Mn(2+) and HCO(3)(-) were replaced by Mg(2+) or Ca(2+) and by formate, oxalate, or acetate, respectively, reveals the specificity of the Mn2+-bicarbonate complexes for the redox interaction with P(+). The results of this work might be considered as experimental evidence for the hypothesis of the participation of Mn(2+) complexes in the evolutionary origin of the inorganic core of the water oxidizing complex of photosystem II.
Asunto(s)
Proteínas Bacterianas/metabolismo , Cloruros/metabolismo , Chloroflexus/metabolismo , Chromatium/metabolismo , Compuestos de Manganeso/metabolismo , Complejo de Proteína del Fotosistema II/metabolismo , Rhodobacter sphaeroides/metabolismo , Proteínas Bacterianas/química , Proteínas Bacterianas/genética , Chloroflexus/química , Chloroflexus/genética , Chloroflexus/efectos de la radiación , Chromatium/química , Chromatium/genética , Chromatium/efectos de la radiación , Cinética , Luz , Oxidación-Reducción , Complejo de Proteína del Fotosistema II/química , Complejo de Proteína del Fotosistema II/genética , Rhodobacter sphaeroides/química , Rhodobacter sphaeroides/genética , Rhodobacter sphaeroides/efectos de la radiaciónRESUMEN
The effects of suppression of the carbonic anhydrase (CA) activity by a CA-inhibitor, acetazolamide (AA), on the photosynthetic activities of photosystem II (PS II) particles from higher plants were investigated. AA along with CA-activity inhibits the PS II photosynthetic electron transfer and the AA-induced suppression is totally reversed by the addition of bicarbonate (3-5 mM). Similar effect of recovery in the PS II photosynthetic activity was also revealed upon the addition of known artificial electron donors (potassium ferrocyanide and TMPD). Significance and possible functions of CA for the PS II donor side are discussed.
Asunto(s)
Acetazolamida/farmacología , Inhibidores de Anhidrasa Carbónica/farmacología , Anhidrasas Carbónicas/química , Pisum sativum/efectos de los fármacos , Acetazolamida/química , Bicarbonatos/farmacología , Inhibidores de Anhidrasa Carbónica/química , Anhidrasas Carbónicas/metabolismo , Clorofila/química , Clorofila/metabolismo , Clorofila A , Transporte de Electrón , Concentración de Iones de Hidrógeno , Cinética , Pisum sativum/enzimologíaRESUMEN
Dependence of the electrochemical potential of oxidation of Mn(II) to Mn(III) on logarithm of bicarbonate concentration at different pH is considered. Slope values of the dependence are equal to -60, -120 and -180mV/log C(HCO)3 at pH6.20, 6.50 and 8.35 respectively, that corresponds to binding of one, two and three HCO(3)(-) ligands to Mn(III). Extrapolation of these dependences to log C(HCO)3=0 shows that at pH6.20 complex [Mn(III)HCO(3)](2+) with E(0)=0.99V and K(st)=6.5×10(8)M(-1), at pH6.50 complex [Mn(III)(HCO(3))(2)](+) with E(0)=0.77V and K(st)=3.5×10(12)M(-2), and at pH8.35 complex [Mn(III)(HCO(3))(3)](0) with E(0)=0.67V and K(st)=1.73×10(14)M(-3) are formed. From the dependence of oxidation potential of Mn(II) to Mn(III) on pH at initial concentration of NaHCO(3) equal to 28mM the limits of pH stability of the complexes were determined: pH5.0-6.35 for [Mn(III)HCO(3)](2+), pH6.35-7.0 for [Mn(III)(HCO(3))(2)](+) and pH7.0-8.35 for [Mn(III)(HCO(3))(3)](0). The obtained data may be important for understanding the mechanism of stimulating action of HCO(3)(-) ions on photoinduced electron transfer from Mn(II) to reaction centres of photosystem2 or to reaction centres of anoxygenic photosynthetic bacteria.
Asunto(s)
Bicarbonatos/química , Complejos de Coordinación/química , Manganeso/química , Complejo de Proteína del Fotosistema II/química , Transporte de Electrón , Concentración de Iones de Hidrógeno , Cinética , Oxidación-Reducción , Complejo de Proteína del Fotosistema II/metabolismoRESUMEN
Four sources of carbonic anhydrase (CA) activity in submembrane preparations of photosystem II (PS II) isolated from pea leaves were examined. Three of them belong to the hydrophilic proteins of the oxygen-evolving complex of PS II with molecular mass 33 kDa (protein PsbO), 24 kDa (protein PsbP), and 18 kDa (protein PsbQ). The fourth source of CA activity is associated with a pigment-protein complex of PS II after removing three hydrophilic proteins by salt treatment. Except for protein PsbQ, the CA activity of all these proteins depends on the presence of Mn2+: the purified protein PsbO did not show CA activity before adding Mn2+ into the medium (concentration of Mn2+ required for 50% effect, EC(50), was 670 microM); CA activity of protein mixture composed of PsbP and PsbQ increased more than 5-fold upon adding Mn2+ (EC(50) was 45 microM). CA activity of purified protein PsbP increased 2-fold in the presence of 200 microM Mn2+. As indicated for the mixture of two proteins (PsbP and PsbQ), Mg2+, Ca2+, and Zn2+, in contrast to Mn2+, suppressed CA activity (both initial and Mn2+-induced activity). Since the found sources of CA activity demonstrated properties different from ones of typical CA (need for Mn2+, insensitivity or low sensitivity to acetazolamide or ethoxyzolamide) and such CA activity was found only among PS II proteins, we cannot exclude that they belong to the type of Mn-dependent CA associated with PS II.
Asunto(s)
Anhidrasas Carbónicas/metabolismo , Manganeso/metabolismo , Complejo de Proteína del Fotosistema II/metabolismo , Pisum sativum/enzimología , Proteínas de Plantas/metabolismo , Anhidrasas Carbónicas/química , Anhidrasas Carbónicas/genética , Anhidrasas Carbónicas/aislamiento & purificación , Cinética , Peso Molecular , Pisum sativum/química , Pisum sativum/genética , Complejo de Proteína del Fotosistema II/química , Complejo de Proteína del Fotosistema II/genética , Complejo de Proteína del Fotosistema II/aislamiento & purificación , Proteínas de Plantas/química , Proteínas de Plantas/genética , Proteínas de Plantas/aislamiento & purificaciónRESUMEN
It is found that dark reduction of photooxidized primary electron donor P870+ in reaction centres from purple anoxygenic bacteria (two non-sulphur Fe-oxidizing Rhodovulum iodosum and Rhodovulum robiginosum, Rhodobacter sphaeroides R-26 and sulphur alkaliphilic Thiorhodospira sibirica) is accelerated upon the addition of Mn2+ jointly with bicarbonate (30-75 mM). The effect is not observed if Mn2+ and HCO3(-) have been replaced by Mg2+ and HCO2(-), respectively. The dependence of the effect on bicarbonate concentration suggests that formation of Mn2+-bicarbonate complexes, Mn(HCO3)+ and/or Mn(HCO3)2, is required for re-reduction of P870+ with Mn2+. The results are considered as experimental evidence for a hypothesis on possible participation of Mn-bicarbonate complexes in the evolutionary origin of oxygenic photosynthesis in the Archean era.