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101.
Leighton H. Daigh Brittany L. Griffin Ali Soroush Murad R. Mamedov John L. Casey 《Journal of virology》2013,87(15):8665-8674
Hepatitis delta virus (HDV) replication and packaging require interactions between the unbranched rodlike structure of HDV RNA and hepatitis delta antigen (HDAg), a basic, disordered, oligomeric protein. The tendency of the protein to bind nonspecifically to nucleic acids has impeded analysis of HDV RNA protein complexes and conclusive determination of the regions of HDAg involved in RNA binding. The most widely cited model suggests that RNA binding involves two proposed arginine-rich motifs (ARMs I and II) in the middle of HDAg. However, other studies have questioned the roles of the ARMs. Here, binding activity was analyzed in vitro using HDAg-160, a C-terminal truncation that binds with high affinity and specificity to HDV RNA segments in vitro. Mutation of the core arginines of ARM I or ARM II in HDAg-160 did not diminish binding to HDV unbranched rodlike RNA. These same mutations did not abolish the ability of full-length HDAg to inhibit HDV RNA editing in cells, an activity that involves RNA binding. Moreover, only the N-terminal region of the protein, which does not contain the ARMs, was cross-linked to a bound HDV RNA segment in vitro. These results indicate that the amino-terminal region of HDAg is in close contact with the RNA and that the proposed ARMs are not required for binding HDV RNA. Binding was not reduced by mutation of additional clusters of basic amino acids. This result is consistent with an RNA-protein complex that is formed via numerous contacts between the RNA and each HDAg monomer. 相似文献
102.
Mamedov N. V. Maslennikov S. P. Solodovnikov A. A. Yurkov D. I. 《Plasma Physics Reports》2020,46(2):217-229
Plasma Physics Reports - For a Penning ion generator, the dependences of the amplitude–time characteristics of the discharge current and the extracted current on the intensity and... 相似文献
103.
104.
The stability of the S(3) and S(2) states of the oxygen evolving complex in photosystem II (PSII) was directly probed by EPR spectroscopy in PSII membrane preparations from spinach in the presence of the exogenous electron acceptor PpBQ at 1, 10, and 20 °C. The decay of the S(3) state was followed in samples exposed to two flashes by measuring the split S(3) EPR signal induced by near-infrared illumination at 5 K. The decay of the S(2) state was followed in samples exposed to one flash by measuring the S(2) state multiline EPR signal. During the decay of the S(3) state, the S(2) state multiline EPR signal first increased and then decreased in amplitude. This shows that the decay of the S(3) state to the S(1) state occurs via the S(2) state. The decay of the S(3) state was biexponential with a fast kinetic phase with a few seconds decay half-time. This occurred in 10-20% of the PSII centers. The slow kinetic phase ranged from a decay half-time of 700 s (at 1 °C) to ~100 s (at 20 °C) in the remaining 80-90% of the centers. The decay of the S(2) state was also biphasic and showed quite similar kinetics to the decay of the S(3) state. Our experiments show that the auxiliary electron donor Y(D) was oxidized during the entire experiment. Thus, the reduced form of Y(D) does not participate to the fast decay of the S(2) and S(3) states we describe here. Instead, we suggest that the decay of the S(3) and S(2) states reflects electron transfer from the acceptor side of PSII to the donor side of PSII starting in the corresponding S state. It is proposed that this exists in equilibrium with Y(Z) according to S(3)Y(Z) ? S(2)Y(Z)(?) in the case of the S(3) state decay and S(2)Y(Z) ? S(1)Y(Z)(?) in the case of the S(2) state decay. Two kinetic models are discussed, both developed with the assumption that the slow decay of the S(3) and S(2) states occurs in PSII centers where Y(Z) is also a fast donor to P(680)(+) working in the nanosecond time regime and that the fast decay of the S(3) and S(2) states occurs in centers where Y(Z) reduces P(680)(+) with slower microsecond kinetics. Our measurements also demonstrate that the split S(3) EPR signal can be used as a direct probe to the S(3) state and that it can provide important information about the redox properties of the S(3) state. 相似文献
105.
M. D. Mamedov V. N. Kurashov I. O. Petrova A. A. Zaspa A. Yu. Semenov 《Biochemistry. Biokhimii?a》2010,75(5):579-584
Transfer of electrons between artificial electron donors diphenylcarbazide (DPC) and hydroxylamine (NH2OH) and reaction center of manganese-depleted photosystem 2 (PS2) complexes was studied using the direct electrometrical method. For the first time it was shown that reduction of redox-active amino acid tyrosine Y z · by DPC is coupled with generation of transmembrane electric potential difference (δΨ). The amplitude of this phase comprised ~17% of that of the δΨ phase due to electron transfer between YZ and the primary quinone acceptor QA. This phase is associated with vectorial intraprotein electron transfer between the DPC binding site on the protein-water interface and the tyrosine Y z · . The slowing of ΔΨ decay in the presence of NH2OH indicates effective electron transfer between the artificial electron donor and reaction center of PS2. It is suggested that NH2OH is able to diffuse through channels with diameter of 2.0–3.0 Å visible in PS2 structure and leading from the protein-water interface to the Mn4Ca cluster binding site with the concomitant electron donation to Y z · . Because the dielectrically-weighted distance between the NH2OH binding site and Y z · is not determined, the transfer of electrons from NH2OH to Y z · could be either electrically silent or contribute negligibly to the observed electrogenicity in comparison with hydrophobic donors. 相似文献
106.
Shelaev IV Gostev FE Nadtochenko VA Shkuropatov AY Zabelin AA Mamedov MD Semenov AY Sarkisov OM Shuvalov VA 《Photosynthesis research》2008,98(1-3):95-103
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(+)Chl(D1)(-), which relaxed within 14 ps as indicated by reversible bleaching of 670-nm band that was tentatively assigned to the Chl(D1) absorption. The subsequent electron transfer from Chl(D1)(-) within 14 ps was accompanied by a development of the radical anion band of Pheo(D1) at 445 nm, attributable to the formation of the secondary radical pair P680(+)Pheo(D1)(-). The key point of this model is that the most blue Q(y) transition of Chl(D1) in RC is allowing an effective stabilization of separated charges. Although an alternative mechanism of charge separation with Chl(D1)* as a primary electron donor and Pheo(D1) 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. 相似文献
107.
This review is focused on the mechanism of photovoltage generation involving the photosystem II turnover. This large integral membrane enzyme catalyzes the light-driven oxidation of water and reduction of plastoquinone. The data discussed in this work show that there are four main electrogenic steps in native complexes: (i) light-induced charge separation between special pair chlorophylls P(680) and primary quinone acceptor Q(A); (ii) P(680)(+) reduction by the redox-active tyrosine Y(Z) of polypeptide D1; (iii) oxidation of Mn cluster by Y(Z)(ox) followed by proton release, and (iv) protonation of double reduced secondary quinone acceptor Q(B). The electrogenicity related to (i) proton-coupled electron transfer between Q(A)(-) and preoxidized non-heme iron (Fe(3+)) in native and (ii) electron transfer between protein-water boundary and Y(Z)(ox) in the presence of redox-dye(s) in Mn-depleted samples, respectively, were also considered. Evaluation of the dielectric properties using the electrometric data and the polarity profiles of reaction center from purple bacteria Blastochloris viridis and photosystem II are presented. The knowledge of the profile of dielectric permittivity along the photosynthetic reaction center is important for understanding of the mechanism of electron transfer between redox cofactors. 相似文献
108.
Electrogenic reduction of the primary electron donor P700 by plastocyanin in photosystem I complexes
Mahir D. Mamedov Aygun A. Mamedova Sergey K. Chamorovsky Alexey Yu. Semenov 《FEBS letters》2001,500(3):172-176
An electrometric technique was used to investigate electron transfer between spinach plastocyanin (Pc) and photooxidized primary electron donor P700 in photosystem I (PS I) complexes from the cyanobacterium Synechocystis sp. PCC 6803. In the presence of Pc, the fast unresolvable kinetic phase of membrane potential generation related to electron transfer between P700 and the terminal iron–sulfur acceptor FB was followed by additional electrogenic phases in the microsecond and millisecond time scales, which contribute approximately 20% to the overall electrogenicity. These phases are attributed to the vectorial electron transfer from Pc to the protein-embedded chlorophyll dimer P700+ within the PsaA/PsaB heterodimer. The observed rate constant of the millisecond kinetic phase exhibited a saturation profile at increasing Pc concentration, suggesting the formation of a transient complex between Pc and PS I with the dissociation constant Kd of about 80 μM. A small but detectable fast electrogenic phase was observed at high Pc concentration. The rate constant of this phase was independent of Pc concentration, indicating that it is related to a first-order process. 相似文献
109.
Mamedov MD Beshta OE Shutilova NI Semenov AY Samuilov VD 《Biochemistry. Biokhimii?a》2000,65(6):728-731
Proteoliposomes containing oxygen-evolving particles of Photosystem II and associated with a planar phospholipid membrane generate a transmembrane electric potential difference (DeltaPsi) induced by a laser flash. With direct electrometrical technique, it was shown that the direction of the electrical field ("minus" inside the proteoliposome) corresponds to acceptor side of the Photosystem II complex facing inside and donor side facing outside of the liposomes. In addition to the fast phase (tau < 0.1 microsec) of the DeltaPsi generation due to electron transfer between YZ of the water-oxidizing complex and the primary plastoquinone QA, a phase with tau approximately 120 microsec and maximum amplitude approximately 30% of the amplitude of the fast phase was observed under the first flash in proteoliposomes containing potassium ferricyanide, which is known as an oxidant of the non-heme iron (Fenh) on the acceptor side of Photosystem II. This additional phase was absent under the second laser flash but was completely restored after 5 min dark adaptation. The phase of the photoelectric response with tau approximately 120 microsec is probably due to electron transfer from QA to Fenh(III) and likely includes a component related to H+ transfer. 相似文献
110.
Semenov AY Vassiliev IR van Der Est A Mamedov MD Zybailov B Shen G Stehlik D Diner BA Chitnis PR Golbeck JH 《The Journal of biological chemistry》2000,275(31):23429-23438
Interruption of the menA or menB gene in Synechocystis sp. PCC 6803 results in the incorporation of a foreign quinone, termed Q, into the A(1) site of photosystem I with a number of experimental indicators identifying Q as plastoquinone-9. A global multiexponential analysis of time-resolved optical spectra in the blue region shows the following three kinetic components: 1) a 3-ms lifetime in the absence of methyl viologen that represents charge recombination between P700(+) and an FeS(-) cluster; 2) a 750-microseconds lifetime that represents electron donation from an FeS(-) cluster to methyl viologen; and 3) an approximately 15-microseconds lifetime that represents an electrochromic shift of a carotenoid pigment. Room temperature direct detection transient EPR studies of forward electron transfer show a spectrum of P700(+) Q(-) during the lifetime of the spin polarization and give no evidence of a significant population of P700(+) FeS(-) for t = 2-3 microseconds. The UV difference spectrum measured 5 microseconds after a flash shows a maximum at 315 nm, a crossover at 280 nm, and a minimum at 255 nm as well as a shoulder at 290-295 nm, all of which are characteristic of the plastoquinone-9 anion radical. Kinetic measurements that monitor Q at 315 nm show a major phase of forward electron transfer to the FeS clusters with a lifetime of approximately 15 microseconds, which matches the electrochromic shift at 485 nm of the carotenoid, as well as an minor phase with a lifetime of approximately 250 microseconds. Electrometric measurements show similar biphasic kinetics. The slower kinetic phase can be detected using time-resolved EPR spectroscopy and has a spectrum characteristic of a semiquinone anion radical. We estimate the redox potential of plastoquinone-9 in the A(1) site to be more oxidizing than phylloquinone so that electron transfer from Q(-) to F(X) is thermodynamically unfavorable in the menA and menB mutants. 相似文献