A.Ya. Shkuropatov

Russian Academy of Sciences, Moskva, Moscow, Russia

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Publications (43)82.61 Total impact

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    Full-text · Dataset · Nov 2015
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    A. A. Zabelin · V. A. Shkuropatova · A. Ya. Shkuropatov · V. A. Shuvalov
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    ABSTRACT: Mid-infrared (4500-1150 cm–1) absorbance changes induced by continuous illumination of Mn-depleted core complexes of photosystem II (PSII) from spinach in the presence of exogenous electron acceptors (potassium ferricyanide and silicomolybdate) were studied by FTIR difference spectroscopy in the temperature range 100–265 K. The FTIR difference spectrum for photooxidation of the chlorophyll dimer P680 was determined from the set of signals associated with oxidation of secondary electron donors (β-carotene, chlorophyll) and reduction of the primary quinone QA. On the basis of analysis of the temperature dependence of the P 680+/P680 FTIR spectrum, it was concluded that frequencies of 131-keto-C=O stretching modes of neutral chlorophyll molecules PD1 and PD2, which constitute P680, are similar to each other, being located at ∼1700 cm–1. This together with considerable difference between the stretching mode frequencies of keto groups of P D1+ and P+D2 cations (1724 and 1709 cm–1, respectively) is in agreement with a literature model (Okubo et al. (2007) Biochemistry, 46, 4390–4397) suggesting that the positive charge in the P 680+ dimer is mainly localized on one of the two chlorophyll molecules. A partial delocalization of the charge between the PD1 and PD2 molecules in P 680+ is supported by the presence of a characteristic electronic intervalence band at ∼3000 cm–1. It is shown that a bleaching band at 1680 cm–1 in the P 680+/P680 FTIR spectrum does not belong to P680. A possible origin of this band is discussed, taking into account the temperature dependence (100–265 K) of light-induced absorbance changes of PSII core complexes in the visible spectral region from 620 to 720 nm.
    Full-text · Article · Oct 2015 · Biochemistry (Moscow)
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    ABSTRACT: Phosphorescence characterized by the main emission band at 952 ± 1 nm (1.30 eV), the lifetime of 1.5 ± 0.1 ms and the quantum yield nearly equal to that for monomeric chlorophyll a in aqueous detergent dispersions, has been detected in isolated reaction centers (RCs) of spinach photosystem II at 77 K. The excitation spectrum shows maxima corresponding to absorption bands of chlorophyll a, pheophytin a, and β-carotene. The phosphorescence intensity strongly depends upon the redox state of RCs. The data suggest that the phosphorescence signal originates from the chlorophyll triplet state populated via charge recombination in the radical pair [Formula: see text].
    No preview · Article · Feb 2015 · Photosynthesis Research
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    ABSTRACT: The native pheophytin a (Pheo a) in isolated reaction centers of Photosystem II (PSII RCs) has been chemically exchanged with extraneous 7-deformyl-7-hydroxymethyl-Pheo b (7(1)-OH-Pheo b) which differs from Pheo a by the C-7 substituent (hydroxymethyl instead of methyl). The two pigments have similar reduction potentials in vitro [M. Meyer, Dissertation, Universität München, 1997], while their absorption spectra show small but distinct differences in the visible region. The resulting 7(1)-OH-Pheo b-modified reaction center preparations were characterized by HPLC, electronic absorption and light-induced FTIR absorption difference spectroscopies, together with photoaccumulation of the reduced pheophytin electron acceptor and NaBH4-treatment. About 70% of the total Pheo a are found to be replaced by 7(1)-OH-Pheo b molecules in modified preparations, indicating that both the photochemically active (PheoD1) and inactive (PheoD2) binding sites were subjected to pigment exchange. The 7(1)-OH-Pheo b molecule located at the PheoD1 site is able to functionally replace the native Pheo a, participating in primary charge separation as an electron acceptor. The Qx absorption band of this modified pheophytin molecule is localized at ~546nm; its Qy band is blue-shifted with respect to the absorption of other reaction center core pigments, being located at ~665nm. The Qy and Qx optical transitions of the 7(1)-OH-Pheo b molecule exchanged into the PheoD2 site are identified at 677 and 543.5nm, respectively. The photochemically active double-modified PS II RCs additionally containing 7-deformyl-7-hydroxymethyl-13(1)-deoxo-13(1)-hydroxy-Pheo b at the PheoD2 site were obtained by treatment of the 7(1)-OH-Pheo b-modified RCs with NaBH4.
    Full-text · Article · Aug 2014 · Biochimica et Biophysica Acta (BBA) - Bioenergetics
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    ABSTRACT: Ultrafast absorption spectroscopy with 20-fs resolution was applied to study primary charge separation in spinach photosystem II (PSII) reaction center (RC) and PSII core complex (RC complex with integral antenna) upon excitation at maximum wavelength 700-710 nm at 278 K. It was found that the initial charge separation between P680* and ChlD1 (Chl-670) takes place with a time constant of ~1 ps with the formation of the primary charge-separated state P680* with an admixture of: P680*((1-δ)) (P680(δ+)ChlD1(δ-)), where δ ~ 0.5. The subsequent electron transfer from P680(δ+)ChlD1(δ-) to pheophytin (Pheo) occurs within 13 ps and is accompanied by a relaxation of the absorption band at 670 nm (ChlD1(δ-)) and bleaching of the PheoD1 bands at 420, 545, and 680 nm with development of the Pheo(-) band at 460 nm. Further electron transfer to QA occurs within 250 ps in accordance with earlier data. The spectra of P680(+) and Pheo(-) formation include a bleaching band at 670 nm; this indicates that Chl-670 is an intermediate between P680 and Pheo. Stimulated emission kinetics at 685 nm demonstrate the existence of two decaying components with time constants of ~1 and ~13 ps due to the formation of P680(δ+)ChlD1(δ-) and P680(+)PheoD1(-), respectively.
    Full-text · Article · Mar 2014 · Biochemistry (Moscow)
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    ABSTRACT: The reaction of the irreversible chemical reduction of the 13(1)-keto C=O group of pheophytin a (Pheo a) with sodium borohydride in reaction centers (RCs) of functionally active spinach photosystem II (PS II) core complexes was studied. Stable, chromatographically purified PS II core complex preparations with altered chromophore composition are obtained in which ~25% of Pheo a molecules are modified to 13(1)-deoxo-13(1)-hydroxy-Pheo a. Some of the chlorophyll a molecules in the complexes were also irreversibly reduced with borohydride to 13(1)-deoxo-13(1)-hydroxy-chlorophyll a. Based on the results of comparative study of spectral, biochemical, and photochemical properties of NaBH4-treated and control preparations, it was concluded that: (i) the borohydride treatment did not result in significant dissociation of the PS II core complex protein ensemble; (ii) the modified complexes retained the ability to photoaccumulate the radical anion of the pheophytin electron acceptor in the presence of exogenous electron donor; (iii) only the photochemically inactive pheophytin PheoD2 is subjected to the borohydride treatment; (iv) the Qx optical transition of the PheoD2 molecule in the RC of PS II core complexes is located at 543 nm; (v) in the Qy spectral region, PheoD2 probably absorbs at ~680 nm.
    Full-text · Article · Apr 2013 · Biochemistry (Moscow)
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    A A Zabelin · V A Shkuropatova · V A Shuvalov · A Ya Shkuropatov
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    ABSTRACT: Photochemical oxidation of the primary electron donor P in reaction centers (RCs) of the filamentous anoxygenic phototrophic bacterium Chloroflexus (C.) aurantiacus was examined by light-induced Fourier transform infrared (FTIR) difference spectroscopy at 95 K in the spectral range of 4000–1200 cm−1. The light-induced P+Q A−/PQA IR spectrum of C. aurantiacus RCs is compared to the well-characterized FTIR difference spectrum of P photooxidation in the purple bacterium Rhodobacter (R.) sphaeroides R-26 RCs. The presence in the P+Q A−/PQA FTIR spectrum of C. aurantiacus RCs of specific low-energy electronic transitions at ∼2650 and ∼2200 cm−1, as well as of associated vibrational (phase-phonon) bands at 1567, 1481, and 1294–1285 cm−1, indicates that the radical cation P+ in these RCs has dimeric structure, with the positive charge distributed between the two coupled bacteriochlorophyll a molecules. The intensity of the P+ absorbance band at ∼1250 nm (upon chemical oxidation of P at room temperature) in C. aurantiacus RCs is approximately 1.5 times lower than that in R. sphaeroides R-26 RCs. This fact, together with the decreased intensity of the absorbance band at ∼2650 cm−1, is interpreted in terms of the weaker coupling of bacteriochlorophylls in the P+ dimer in C. aurantiacus compared to R. sphaeroides R-26. In accordance with the previous (pre)resonance Raman data, FTIR measurements in the carbonyl stretching region show that in C. aurantiacus RCs (i) the 131-keto C=O groups of PA and PB molecules constituting the P dimer are not involved in hydrogen bonding in either neutral or photooxidized state of P and (ii) the 31-acetyl C=O group of PB forms a hydrogen bond (probably with tyrosine M187) absorbing at 1635 cm−1. Differential signals at 1757(+)/1749(−) and 1741(+)/1733(−) cm−1 in the FTIR spectrum of C. aurantiacus RCs are attributed to the 133-ester C=O groups of P in different environments.
    Full-text · Article · Feb 2012 · Biochemistry (Moscow)
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    V V Terentyev · A Ya Shkuropatov · V A Shkuropatova · V A Shuvalov · V V Klimov
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    ABSTRACT: 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.
    Full-text · Article · Dec 2011 · Biochemistry (Moscow)
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    A G Yakovlev · L G Vasilieva · A Y Shkuropatov · V A Shuvalov
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    ABSTRACT: Primary stage of charge separation and transfer of charges was studied in reaction centers (RCs) of point mutants LL131H and LL131H/LM160H/FM197H of the purple bacterium Rhodobacter sphaeroides by differential absorption spectroscopy with temporal resolution of 18 fsec at 90 K. Difference absorption spectra measured at 0–4 psec delays after excitation of dimer P at 870 nm with 30 fsec step were obtained in the spectral range of 935–1060 nm. It was found that a decay of P* due to charge separation is considerably slower in the mutant RCs in comparison with native RCs of Rba. sphaeroides. Coherent oscillations were found in the kinetics of stimulated emission of the P* state at 940 nm. Fourier analysis of the oscillations revealed a set of characteristic bands in the frequency range of 20–500 cm−1. The most intense band has the frequency of −30 cm−1 in RCs of mutant LL131H and in native RCs and the frequency of ∼100 cm−1 in RCs of the triple mutant. It was found that an absorption band of bacteriochlorophyll anion B A− which is registered in the difference absorption spectra of native RCs at 1020 nm is absent in the analogous spectra of the mutants. The results are analyzed in terms of the participation of the BA molecule in the primary electron transfer in the presence of a nuclear wave packet moving along the inharmonic surface of P* potential energy.
    Full-text · Article · Oct 2011 · Biochemistry (Moscow)
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    ABSTRACT: Mid-infrared spectral changes associated with the photoreduction of the bacteriopheophytin electron acceptor H(A) in reaction centers (RCs) of the filamentous anoxygenic phototrophic bacterium Chloroflexus (Cfl.) aurantiacus are examined by light-induced Fourier transform infrared (FTIR) spectroscopy. The light-induced H(A)(-)/H(A) FTIR (1800-1200cm(-1)) difference spectrum of Cfl. aurantiacus RCs is compared to that of the previously well characterized purple bacterium Rhodobacter (Rba.) sphaeroides RCs. The most notable feature is that the large negative IR band at 1674cm(-1) in Rba. sphaeroides R-26, attributable to the loss of the absorption of the 13(1)-keto carbonyl of H(A) upon the radical anion H(A)(-) formation, exhibits only a very minor upshift to 1675cm(-1) in Cfl. aurantiacus. In contrast, the absorption band of the 13¹-keto C=O of H(A)(-) is strongly upshifted in the spectrum of Cfl. aurantiacus compared to that of Rba. sphaeroides (from 1588 to 1623cm(-1)). The data are discussed in terms of: (i) replacing the glutamic acid at L104 in Rba. sphaeroides R-26 RCs by a weaker hydrogen bond donor, a glutamine, at the equivalent position L143 in Cfl. aurantiacus RCs; (ii) a strengthening of the hydrogen-bonding interaction of the 13¹-keto C=O of H(A) with Glu L104 and Gln L143 upon H(A)(-) formation and (iii) a possible influence of the protein dielectric environment on the 13¹-keto C=O stretching frequency of neutral H(A). A conformational heterogeneity of the 13³-ester C=O group of H(A) is detected for Cfl. aurantiacus RCs similar to what has been previously described for purple bacterial RCs.
    Full-text · Article · May 2011 · Biochimica et Biophysica Acta
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    ABSTRACT: Low temperature (77-90 K) measurements of absorption spectral changes induced by red light illumination in isolated photosystem II (PSII) reaction centers (RCs, D1/D2/Cyt b559 complex) with different external acceptors and in PSII core complexes have shown that two different electron donors can alternatively function in PSII: chlorophyll (Chl) dimer P(680) absorbing at 684 nm and Chl monomer Chl(D1) absorbing at 674 nm. Under physiological conditions (278 K) transient absorption difference spectroscopy with 20-fs resolution was applied to study primary charge separation in spinach PSII core complexes excited at 710 nm. It was shown that the initial electron transfer reaction takes place with a time constant of ~0.9 ps. This kinetics was ascribed to charge separation between P(680)* and Chl(D1) absorbing at 670 nm accompanied by the formation of the primary charge-separated state P(680)(+)Chl(DI)(-), as indicated by 0.9-ps transient bleaching at 670 nm. The subsequent electron transfer from Chl(D1)(-) occurred within 13-14 ps and was accompanied by relaxation of the 670-nm band, bleaching of the Pheo(D1) Q(x) absorption band at 545 nm, and development of the anion-radical band of Pheo(D1)(-) at 450-460 nm, the latter two attributable to formation of the secondary radical pair P(680)(+)Pheo(D1)(-). The 14-ps relaxation of the 670-nm band was previously assigned to the Chl(D1) absorption in isolated PSII RCs [Shelaev, Gostev, Nadtochenko, Shkuropatov, Zabelin, Mamedov, Semenov, Sarkisov and Shuvalov, Photosynth. Res. 98 (2008) 95-103]. We suggest that the longer wavelength position of P(680) (near 680 nm) as a primary electron donor and the shorter wavelength position of Chl(D1) (near 670 nm) as a primary acceptor within the Q(y) transitions in RC allow an effective competition with an energy transfer and stabilization of separated charges. Although an alternative mechanism of charge separation with Chl(D1)* as the primary electron donor and Pheo(D1) as the primary acceptor cannot be ruled out, the 20-fs excitation at the far-red tail of the PSII core complex absorption spectrum at 710 nm appears to induce a transition to a low-energy state P(680)* with charge-transfer character (probably P(D1)(δ+)P(D2)(δ-)) which results in an effective electron transfer from P(680)* (the primary electron donor) to Chl(D1) as the intermediary acceptor.
    Full-text · Article · Mar 2011 · Journal of photochemistry and photobiology. B, Biology
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    ABSTRACT: The role of tyrosine M210 in charge separation and stabilization of separated charges was studied by analyzing of the femtosecond oscillations in the kinetics of decay of stimulated emission from P*and of a population of the primary charge separated state P+B-A in YM210L and YM210L/HL168L mutant reaction centers (RCs) of Rhodobacter sphaeroides in comparison with those in native Rba. sphaeroides RCs. In the mutant RCs, TyrM210 was replaced by Leu. The HL168L mutation placed the redox potential of the P+/P pair 123 mV below that of native RCs, thus creating a theoretical possibility of P+BA- stabilization. Kinetics of P*decay at 940 nm of both mutants show a significant slowing of the primary charge separation reaction in comparison with native RCs. Distinct damped oscillations in these kinetics with main frequency bands in the range of 90-150 cm-1 reflect mostly nuclear motions inside the dimer P. Formation of a very small absorption band of B A- at 1020 nm is registered in RCs of both mutants. The formation of the B A- band is accompanied by damped oscillations with main frequencies from ∼10 to ∼150 cm-1. Only a partial stabilization of the P+B A- state is seen in the YM210L/HL168L mutant in the form of a small non-oscillating background of the 1020-nm kinetics. A similar charge stabilization is absent in the YM210L mutant. A model of oscillatory reorientation of the OH-group of TyrM210 in the electric fields of P+ and B A- is proposed to explain rapid stabilization of the P+B A- state in native RCs. Small oscillatory components at ∼330-380 cm-1 in the 1020-nm kinetics of native RCs are assumed to reflect this reorientation. We conclude that the absence of TyrM210 probably cannot be compensated by lowering of the P+B A- free energy that is expected for the double YM210L/HL168L mutant. An oscillatory motion of the HOH55 water molecule under the influence of P+ and B A- is assumed to be another potential contributor to the mechanism of P+B A- stabilization.
    Preview · Article · Jul 2010 · Biochemistry (Moscow)
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    A G Yakovlev · L G Vasilieva · A Y Shkuropatov · V A Shuvalov
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    ABSTRACT: Difference femtosecond absorption spectroscopy with 20-fsec temporal resolution was applied to study a primary stage of charge separation and transfer processes in reaction centers of YM210L and YM210L/FM197Y site-directed mutants of the purple bacterium Rhodobacter sphaeroides at 90 K. Photoexcitation was tuned to the absorption band of the primary electron donor P at 880 nm. Coherent oscillations in the kinetics of stimulated emission of P* excited state at 940 nm and of anion absorption of monomeric bacteriochlorophyll B(A)(-) at 1020 nm were monitored. The absence of tyrosine YM210 in RCs of both mutants leads to strong slowing of the primary reaction P* --> P(+)B(A)(-) and to the absence of stabilization of separated charges in the state P(+)B(A)(-). Mutation FM197Y increases effective mass of an acetyl group of pyrrole ring I in the bacteriochlorophyll molecule P(B) of the double mutant YM210L/FM197Y by a hydrogen bond with OH-TyrM197 group that leads to a decrease in the frequency of coherent nuclear motions from 150 cm(-1) in the single mutant YM210L to ~100 cm(-1) in the double mutant. Oscillations with 100-150 cm(-1) frequencies in the dynamics of the P* stimulated emission and in the kinetics of the reversible formation of P(+)B(A)(-) state of both mutants reflect a motion of the P(B) molecule relatively to P(A) in the area of mutual overlapping of their pyrrole rings I. In the double mutant YM210L/FM197Y the oscillations in the P* emission band and the B(A)(-) absorption band are conserved within a shorter time ~0.5 psec (1.5 psec in the YM210L mutant), which may be a consequence of an increase in the number of nuclei forming a wave packet by adding a supplementary mass to the dimer P.
    Full-text · Article · Nov 2009 · Biochemistry (Moscow)
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    ABSTRACT: Difference absorption spectroscopy with temporal resolution of approximately 20 fsec was used to study the primary phase of charge separation in isolated reaction centers (RCs) of Chloroflexus aurantiacus at 90 K. An ensemble of difference (light-minus-dark) absorption spectra in the 730-795 nm region measured at -0.1 to 4 psec delays relative to the excitation pulse was analyzed. Comparison with analogous data for RCs of HM182L mutant of Rhodobacter sphaeroides having the same pigment composition identified the 785 nm absorption band as the band of bacteriopheophytin Phi(B) in the B-branch. By study the bleaching of this absorption band due to formation of Phi(B)(-), it was found that a coherent electron transfer from P* to the B-branch occurs with a very small delay of 10-20 fsec after excitation of dimer bacteriochlorophyll P. Only at 120 fsec delay electron transfer from P* to the A-branch occurs with the formation of bacteriochlorophyll anion B(A)(-) absorption band at 1028 nm and the appearance of P* stimulated emission at 940 nm, as also occurs in native RCs of Rb. sphaeroides. It is concluded that a nuclear wave packet motion on the potential energy surface of P* after a 20-fsec light pulse excitation leads to the coherent formation of the P(+)Phi(B)(-) and P(+)B(A)(-) states.
    No preview · Article · Aug 2009 · Biochemistry (Moscow)
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    ABSTRACT: Methods of photoinduced Fourier transform infrared (FTIR) difference spectroscopy and circular dichroism were employed for studying features of pigment-protein interactions caused by replacement of isoleucine L177 by histidine in the reaction center (RC) of the site-directed mutant I(L177)H of Rhodobacter sphaeroides. A functional state of pigments in the photochemically active cofactor branch was evaluated with the method of photo-accumulation of reduced bacteriopheophytin H A−. The results are compared with those obtained for wild-type RCs. It was shown that the dimeric nature of the radical cation of the primary electron donor P was preserved in the mutant RCs, with an asymmetric charge distribution between the bacteriochlorophylls PA and PB in the P+ state. However, the dimers P in the wild-type and mutant RCs are not structurally identical due probably to molecular rearrangements of the PA and PB macrocycles and/or alterations in their nearest amino acid environment induced by the mutation. Analysis of the electronic absorption and FTIR difference P+Q−/PQ spectra suggests the 173-ester group of the bacteriochlorophyll PA to be involved in covalent interaction with the I(L177)H RC protein. Incorporation of histidine into the L177 position does not modify the interaction between the primary electron acceptor bacteriochlorophyll BA and the bacteriopheophytin HA. Structural changes are observed in the monomer bacteriochlorophyll BB binding site in the inactive chromophore branch of the mutant RCs.
    No preview · Article · Feb 2009 · Biochemistry (Moscow)
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    ABSTRACT: In Part I of the article, a review of recent data on electron-transfer reactions in photosystem II (PSII) and bacterial reaction center (RC) has been presented. In Part II, transient absorption difference spectroscopy with 20-fs resolution was applied to study the primary charge separation in PSII RC (DI/DII/Cyt b 559 complex) excited at 700 nm at 278 K. It was shown that the initial electron-transfer reaction occurs within 0.9 ps with the formation of the charge-separated state P680+ChlD1−, which relaxed within 14 ps as indicated by reversible bleaching of 670-nm band that was tentatively assigned to the ChlD1 absorption. The subsequent electron transfer from ChlD1− within 14 ps was accompanied by a development of the radical anion band of PheoD1 at 445 nm, attributable to the formation of the secondary radical pair P680+PheoD1−. The key point of this model is that the most blue Q y transition of ChlD1 in RC is allowing an effective stabilization of separated charges. Although an alternative mechanism of charge separation with ChlD1* as a primary electron donor and PheoD1 as a primary acceptor can not be ruled out, it is less consistent with the kinetics and spectra of absorbance changes induced in the PSII RC preparation by femtosecond excitation at 700 nm.
    No preview · Article · Nov 2008 · Photosynthesis Research
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    ABSTRACT: In this work, we report the unique case of bacteriochlorophyll (BChl) - protein covalent attachment in a photosynthetic membrane complex caused by a single mutation. The isoleucine L177 was substituted by histidine in the photosynthetic reaction center (RC) of Rhodobacter sphaeroides. Pigment analysis revealed that one BChl molecule was missing in the acetone-methanol extract of the I(L177)H RCs. SDS-PAGE demonstrated that this BChl molecule could not be extracted with organic solvents apparently because of its stable covalent attachment to the mutant RC L-subunit. Our data indicate that the attached bacteriochlorophyll is one of the special pair BChls, P(A). The chemical nature of this covalent interaction remains to be identified.
    Full-text · Article · Jan 2008 · FEBS Letters
  • Vladimir A. Shuvalov · Andrei G. Yakovlev · L. G. Vasilieva · Anatoly Ya. Shkuropatov
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    ABSTRACT: The mechanism of charge separation and the stabilization of separated charges in photosystem I (PS I) is considered in comparison with reaction centers (RCs) in bacteria. The analysis of the X-ray crystal structures of the RCs together with psec and fsec studies of charge separation coupled to nuclear motion in the system provides new insight into the problem. A psec study of PS I RCs has shown that the primary charge separation takes place between P700*. and the A-A0 complex. The three-dimensional structure of both the primary electron donor and acceptor shows a possible pathway for electron transfer between P700 and the A-A0 complex that is governed by nuclear motions. A fsec study of a coherent formation of the nuclear wavepacket on the potential energy surface of the excited state of the primary electron donor P* and of the charge separated state P+A− (where A is the primary electron acceptor) in native, pheophytin-modified and mutant reaction centers of Rhodobacter spaeroides was compared with X-ray and psec data for PS I RCs. A mechanism of the charge separation and stabilization of separated charges in PS I RCs is proposed.
    No preview · Chapter · May 2007

  • No preview · Article · Jan 2006
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    ABSTRACT: Energy and electron transfer in Photosystem II reaction centers in which the photochemically inactive pheophytin had been replaced by 13(1)-deoxo-13(1)-hydroxy pheophytin were studied by femtosecond transient absorption-difference spectroscopy at 77 K and compared to the dynamics in untreated reaction center preparations. Spectral changes induced by 683-nm excitation were recorded both in the Q(Y) and in the Q(X) absorption regions. The data could be described by a biphasic charge separation. In untreated reaction centers the major component had a time constant of 3.1 ps and the minor component 33 ps. After exchange, time constants of 0.8 and 22 ps were observed. The acceleration of the fast phase is attributed in part to the redistribution of electronic transitions of the six central chlorin pigments induced by replacement of the inactive pheophytin. In the modified reaction centers, excitation of the lowest energy Q(Y) transition produces an excited state that appears to be localized mainly on the accessory chlorophyll in the active branch (B(A) in bacterial terms) and partially on the active pheophytin H(A). This state equilibrates in 0.8 ps with the radical pair. B(A) is proposed to act as the primary electron donor also in untreated reaction centers. The 22-ps (pheophytin-exchanged) or 33-ps (untreated) component may be due to equilibration with the secondary radical pair. Its acceleration by H(B) exchange is attributed to a faster reverse electron transfer from B(A) to. After exchange both and are nearly isoenergetic with the excited state.
    Full-text · Article · Apr 2004 · Biophysical Journal

Publication Stats

507 Citations
82.61 Total Impact Points

Institutions

  • 1986-2015
    • Russian Academy of Sciences
      • • Puschino Institute of Basic Biological Problems
      • • Institute of Soil Science and Photosynthesis
      Moskva, Moscow, Russia
  • 2003
    • Institute of Biological Problems of the North
      Moskovskaya, Stavropol'skiy, Russia
  • 2002
    • Lomonosov Moscow State University
      Moskva, Moscow, Russia