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1.
Increases in the chlorophyll fluorescence Fo (dark level fluorescence) during heat treatments were studied in various higher plants. Besides the dissociation of light-harvesting chlorophyll a/b protein complexes from the reaction center complex of PS II and inactivation of PS II, dark reduction of QA via plastoquinone (PQ) seemed to be related to the Fo increase at high temperatures. In potato leaves or green tobacco cultured cells, a part of the Fo increase was quenched by light, reflecting light-induced oxidation of QA - which had been reduced in the dark at high temperatures. Appearance of the Fo increase due to QA reduction depended on the plant species, and the mechanisms for this are proposed. The reductants seemed to be already present and formed by very brief illumination of the leaves at high temperatures. A ndhB-less mutant of tobacco showed that complex I type NAD(P)H dehydrogenase is not involved in the heat-induced reduction of QA. Quite strong inhibition of the QA reduction by diphenyleneiodonium suggests that a flavoenzyme is one of the electron mediator to PQ from the reductant in the stroma. Reversibility of the heat-induced QA reduction suggests that an enzyme(s) involved is activated at high temperatures and mostly returns to an inactive form at room temperature (25 °C).This revised version was published online in October 2005 with corrections to the Cover Date.  相似文献   

2.
Effects of photoinhibition on photosynthesis in pea (Pisum sativum L.) leaves were investigated by studying the relationship between the severity of a photoinhibitory treatment (measured as Fv/Fm) and several photoacoustic and chlorophyll a fluorescence parameters. Because of the observed linear relationship between the decline of Fv/Fm and the potential oxygen evolution rate determined by the photoacoustic method, the parameter Fv/Fm was used as an indicator for the severity of photoinhibition. Our analysis revealed that part of the Photosystem II (PS II) reaction centers is inactive in oxygen evolution and is also less sensitive to photoinhibition. Correcting the parameter qP (fraction of open PS II reaction centers) for inactive PS II centers unveiled a strong increase of qP in severely inhibited pea leaves, indicating that the inactivated active centers do no longer contribute to qP and that photoinhibition has an all or none effect on PS II centers. Analysis of qE (energy quenching) demonstrated its initial increase possibly associated with dephosphorylation of LHC II. Analysis of qI (photoinhibition dependent quenching) showed that the half-time of recovery of qI increases steeply below an Fv/Fm of 0.65. This increase of the relaxation half-time corresponds with a decrease of the electron transport rate J and tentatively indicates that the supply of ATP, needed for the recovery, starts to decrease. The data indicate the necessity of correcting for inactive centers in order to make valuable conclusions about effects of photoinhibition on photosynthetic parameters.  相似文献   

3.
The nature of excitation energy transfer and charge separation in isolated Photosystem II reaction centers is an area of considerable interest and controversy. Excitation energy transfer from accessory chlorophyll a to the primary electron donor P680 takes place in tens of picoseconds, although there is some evidence that thermal equilibration of the excitation between P680 and a subset of the accessory chlorophyll a occurs on a 100-fs timescale. The intrinsic rate for charge separation at low temperature is accepted to be ca. (2 ps)–1, and is based on several measurements using different experimental techniques. This rate is in good agreement with estimates based on larger sized particles, and is similar to the rate observed with bacterial reaction centers. However, near room temperature there is considerable disagreement as to the observed rate for charge separation, with several experiments pointing to a ca. (3 ps)–1 rate, and others to a ca. (20 ps)-1 rate. These processes and the experiments used to measure them will be reviewed.Abbreviations Chl chlorophyll - FWHM full-width at half-maximum - Pheo pheophytin - PS II Photosystem II - P680 primary electron donor of the Photosystem II reaction center - RC reaction center The US Government right to retain a non-exclusive, royalty free licence in and to any copyright is acknowledged.  相似文献   

4.
Activities of oxygen evolution, fluorescence Fv (a variable part of chlorophyll fluorescence) values, and amounts of the 33 kDa protein remaining bound to the thylakoids in intact spinach chloroplasts were measured during and after high-temperature treatment. The following results were obtained. (1) Both the Fv value and the flash-induced oxygen evolution measured by an oxygen electrode were decreased at high temperatures, but they showed partial recovery when the samples were cooled down and incubated at 25°C for 5 min after high-temperature treatment. (2) Oxygen evolution was more sensitive to high temperatures than the Fv value, and the decrease in the Fv/Fm ratio at high temperatures rather corresponded to that in the oxygen evolution measured at 25°C after high-temperature treatment. (3) Photoinactivation of PS II was very rapid at high temperatures, and this seems to be a cause of the difference between the Fv values and the oxygen-evolving activities at high temperatures. (4) At around 40°C, the manganese-stabilizing 33 kDa protein of PS II was supposed to be released from the PS II core complexes during heat treatment and to rebind to the complexes when the samples were cooled down to 25°C. (5) At higher temperatures, the charge separation reaction of PS II was inactivated, and the PS II complexes became less fluorescent, which was recovered partially at 25°C. (6) Increases in the Fv value due to a large decrease in the electron flow from QA to QB became prominent after high-temperature treatment at around 50°C. This was the main cause of the discrepancy between the Fv values and the oxygen-evolving activities measured at 25°C. Relationship between the process of heat inactivation of PS II reaction center complexes and the fluorescence levels is discussed.  相似文献   

5.
Electron transfer processes in leaves were investigated by chlorophyll fluorescence decay measurements. A fast chlorophyll fluorescence decay was observed in the intact state, reflecting normal electron transfer in Photosystem II. After treatment with DCMU a slow chlorophyll fluorescence decay was measured due to blocked electron transfer after the primary quinone QA. Additional saturating light pulses, one between each two measuring pulses, were used to completely reduce QA of the intact leaf: the chlorophyll fluorescence decay became similar to that of a DCMU treated leaf. A decreased electron donation rate to the reaction centre P680 was obtained after treatment with hydroxylamine. The intensity of the additional saturating light pulses was not sufficient to reduce all QA under this condition and only a small increase of the average chlorophyll fluorescence decay time occurred. Following our previous paper [Berg et al. (1997) Photosynthetica 34, in press], we investigated the effects of water stress with the additional saturating light pulses. An almost complete reduction of QA was possible after water stress started. A small, but systematic shortening of the slow chlorophyll fluorescence decay followed, up to a relative loss of leaf mass of 80%. At this time a rapid shortening of the chlorophyll fluorescence decay occurred, caused by an electron deficiency at the donor site of PS II. Additional saturating light pulses had no effects on the chlorophyll fluorescence decay any more, revealing a radiationless recombination between the reduced primary quinone Q and the oxidized reaction centre P680+.  相似文献   

6.
Oxygen evolving photosystem II particles were exposed to 100 and 250 W m–2 white light at 20°C under aerobic, anaerobic and strongly reducing (presence of dithionite) conditions. Three types of photoinactivation processes with different kinetics could be distinguished: (1) The fast process which occurs under strongly reducing (t 1/21–3 min) and anaerobic conditions (t 1/24–12 min). (2) The slow process (t 1/215–40 min) and (3) the very slow process (t 1/2>100 min), both of which occur under all three sets of conditions.The fast process results in a parallel decline of variable fluorescence (F v) and of Hill reaction rate, accompanied by an antiparallel increase of constant fluorescence (F o). We assume that trapping of QA in a negatively charged stable state, (QA )stab, is responsible for the effects observed.The slow process is characterized by a decline of maximal fluorescence (F m). In presence of oxygen this decline is due to the well known disappearance of F v which proceeds in parallel with the inhibition of the Hill reaction; F o remains essentially constant. Under anaerobic and reducing conditions the decline of F m represents the disappearance of the increment in F o generated by the fast process. We assume that the slow process consists in neutralization of the negative charge in the domain of QA in a manner that renders QA non-functional. The charge separation in the RC is still possible, but energy of excitation becomes thermally dissipated.The very slow photoinactivation process is linked to loss of charge separation ability of the PS II RC and will be analyzed in a forthcoming paper.Abbreviations F chlorophyll a fluorescence - F o, F v, F m constant, variable, maximum fluorescence - F o, F v, F m the same, measured in presence of dithionite (F v suppression method) - PS II photosystem II - RC reaction centre (P680. Pheo) - P680 primary electron donor - Pheo pheophytin, intermediary electron acceptor - QA, QB the primary and secondary electron acceptor - Z, D electron donors to P680 - (QA)stab, (QA H)stab hypothetical modifications of QA resulting from photoinactivation - O-, A- and R-conditions aerobic, anaerobic and strongly reducing (presence of dithionite) conditions - MES 2-(N-morpholine) ethanesulphonic acid - DCPIP 2,6-dichlorphenolindophenol - GGOC mixture of glucose, glucose oxidase and catalase - DT-20 oxygen-evolving PS II particles  相似文献   

7.
The possibility of a Photosystem II (PS II) cyclic electron flow via Cyt b-559 catalyzed by carbonylcyanide m-chlorophenylhydrazone (CCCP) was further examined by studying the effects of the PS II electron acceptor 2,6-dichloro-p-benzoquinone (DCBQ) on the light-induced changes of the redox states of Cyt b-559. Addition to barley thylakoids of micromolar concentrations of DCBQ completely inhibited the changes of the absorbance difference corresponding to the photoreduction of Cyt b-559 observed either in the presence of 10 M ferricyanide or after Cyt b-559 photooxidation in the presence of 2 M CCCP. In CCCP-treated thylakoids, the concentration of photooxidized Cyt b-559 decreased as the irradiance of actinic light increased from 2 to 80 W m-2 but remained close to the maximal concentration (0.53 photooxidized Cyt b-559 per photoactive Photosystem II) in the presence of 50 M DCBQ. The stimulation of Cyt b-559 photooxidation in parallel with the inhibition of its photoreduction caused by DCBQ demonstrate that the extent of the light-induced changes of the redox state of Cyt b-559 in the presence of CCCP is determined by the difference between the rates of photooxidation and photoreduction of Cyt b-559 occuring simultaneously in a cyclic electron flow around PS II.We also observed that the Photosystem I electron acceptor methyl viologen (MV) at a concentration of 1 mM barely affected the rate and extent of the light-induced redox changes of Cyt b-559 in the presence of either FeCN or CCCP. Under similar experimental conditions, MV strongly quenched Chl-a fluorescence, suggesting that Cyt b-559 is reduced directly on the reducing side of Photosystem II.Abbreviations ADRY acceleration of the deactivation reactions of the water-splitting system Y - ANT-2p 2-(3-chloro-4-trifluoromethyl)anilino-3,5-dinitrothiophene - CCCP carbonylcyanide-m-chlorophenylhydrazone - DCBQ 2,6-dichloro-p-benzoquinone - FeCN ferricyanide - MV methyl viologen - P680 Photosystem II reaction center Chl-a dimer CIW-DPB publication No. 1118.  相似文献   

8.
Oxygen-evolving PS II particles from the thermophilic cyanobacterium Synechococcus elongatus are partially purified by centrifugation on a sucrose gradient and are bound to a Chelating Sepharose column loaded with Cu2+ ions. Bound particles are then transformed into PS II RC complexes by two washing steps. First, washing with a phosphate buffer (pH=6.5) containing 0.02% of SB 12 removes the rest of phycobilins and leaves pure PS II core particles on the column. Second, washing with a phosphate buffer (pH=6.2) containing 0.2 M LiClO4 and 0.05% of DM removes CP 47 and CP 43 and leaves bare PS II RC complexes on the column. These are then eluted with a phosphate buffer containing 1% of dodecylmaltoside (DM). The molar ratio of pigments in the eluate changes with the progress of elution but around the middle of the elution period a nearly stable ratio is maintained of Chl a: Pheo a: Car: Cyt b 559 equal to 2.9: 1: 0.9: 0.8. In these fractions the photochemical separation of charges could be demonstrated by accumulation of reduced pheophytin (A of 430–440 nm) and by the flash induced formation of P680+ (A at 820 nm). The relatively slow relaxation kinetics of the latter signal (t1/2 1 ms) may suggest that in a substantial fraction of the RCs QA remains bound to the complex.Abbreviations Car -carotene - Chl a chlorophyll a - CP43, CP47 chlorophyll-proteins, with Rm 43 and 47 kDa - DBMIB dibromothymoquinone,2,5-dibromo-3-methyl-6-isopropyl-1,4-benzoquinone - DM -dodecyl-d-maltoside - HPLC high-performance liquid chromatography - OG n-octyl--d-glucopyranoside - IMAC immobilied metal affinity chromatography - Pheo a pheophytin a - PQ-9 plastoquinone-9 - P680 primary electron donor in PS II - PS II RC Photosystem II reaction centre - QA primary electron acceptor in PS II - SB-12 N-dodecyl-N,N-dimethyl-3-amino-1-propanesulphonate, (sulphobetain 12)  相似文献   

9.
Inhibition of Photosystem II (PS II) activity induced by continuous light or by saturating single turnover flashes was investigated in Ca2+-depleted, Mn-depleted and active PS II enriched membrane fragments. While Ca2+- and Mn-depleted PS II were more damaged under continuous illumination, active PS II was more susceptible to flash-induced photoinhibition. The extent of photoinactivation as a function of the duration of the dark interval between the saturating single turnover flashes was investigated. The active centres showed the most photodamage when the time interval between the flashes was long enough (32 s) to allow for charge recombination between the S2 or S3 and QB to occur. Illumination with groups of consecutive flashes (spacing between the flashes 0.1 s followed by 32 s dark interval) resulted in a binary oscillation of the loss of PS II-activity in active samples as has been shown previously (Keren N, Gong H, Ohad I (1995), J Biol Chem 270: 806–814). Ca2+- and Mn-depleted PS II did not show this effect. The data are explained by assuming that charge recombination in active PS II results in a back reaction that generates P680 triplet and thence singlet oxygen, while in Ca2+- and Mn-depleted PS II charge recombination occurs through a different pathway, that does not involve triplet generation. This correlates with an up-shift of the midpoint potential of QA in samples lacking Ca2+ or Mn that, in term, is predicted to result in the triplet generating pathway becoming thermodynamically less favourable (G.N. Johnson, A.W. Rutherford, A. Krieger, 1995, Biochim. Biophys. Acta 1229, 201–207). The diminished susceptibility to flash-induced photoinhibition in Ca2+- and Mn-depleted PS II is attributed at least in part to this mechanism. This revised version was published online in June 2006 with corrections to the Cover Date.  相似文献   

10.
Pheophytin a (Pheo) in Photosystem II reaction centres was exchanged for 131-deoxo-131-hydroxy-pheophytin a (131-OH-Pheo). The absorption bands of 131-OH-Pheo are blue-shifted and well separated from those of Pheo. Two kinds of modified reaction centre preparations can be obtained by applying the exchange procedure once (RC) or twice (RC). HPLC analysis and Pheo QX absorption at 543 nm show that in RC about 50% of Pheo is replaced and in RC about 75%. Otherwise, the pigment and protein composition are not modified. Fluorescence emission and excitation spectra show quantitative excitation transfer from the new pigment to the emitting chlorophylls. Photoaccumulation of Pheo is unmodified in RC and decreased only in RC, suggesting that the first exchange replaces the inactive and the second the active Pheo. Comparing the effects of the first and the second replacement on the absorption spectrum at 6 K did not reveal substantial spectral differences between the active and inactive Pheo. In both cases, the absorption changes in the QY region can be interpreted as a combination of a blue shift of a transition at 684 nm, a partial decoupling of chlorophylls absorbing at 680 nm and a disappearance of Pheo absorption in the 676-680 nm region. No absorption decrease is observed at 670 nm for RC or RC, showing that neither of the two reaction centre pheophytins contributes substantially to the absorption at this wavelength. This revised version was published online in June 2006 with corrections to the Cover Date.  相似文献   

11.
With a portable PAM-2000 fluorometer it was observed that responses of initial chlorophyll fluorescence Fo level to strong light were different in various plant species examined. When the photochemical efficiency of Photosystem II, Fv/Fm, declined, Fo increased significantly in leaves of some plants such as soybean and cotton, while Fo decreased remarkably in other plants such as wheat and barley. In order to explore the mechanism of the increase in Fo in soybean leaves, the change in D1 protein amount and effects of lincomycin and far-red light on these fluorescence parameters were observed by SDS–PAGE combined with gel scanning and chlorophyll fluorescence analysis. The following results were obtained. (1) The amount of inactive PS II reaction centers increased under strong light and decreased during subsequent dark recovery [Hong and Xu (1997) Chinese Sci Bull 42(8): 684–689]. (2) No net loss of D1 protein occurred after strong light treatment. (3) Lincomycin taken up through petioles following strong light treatment had no significant effect on D1 protein level and the decay of Fo in the dark. (4) Far-red light applied after strong light treatment could largely attenuate the increase in Fo and accelerate Fo decay in the dark. Based on these results, it is deduced that the increase in Fo under strong light is mainly due to reversible inactivation of part of PS II reaction centers, rather than the net loss of D1 protein and that reversible inactivation of PS II is prevalent in some plants.  相似文献   

12.
The sensitivity of the D-1 and D-2 polypeptide subunits of photosystem II towards trypsin treatment of the thylakoid membrane has been probed with specific antibodies. As long known, electron flow from water to ferricyanide becomes inhibitor insensitive after this trypsin treatment. We show that under these conditions the D-2 polypeptide is cut by trypsin at arg 234. Also the D-1 polypeptide is cut, probably at arg 238. When short time trypsination of the membrane is done in the presence of inhibitors, electron flow also becomes inhibitor insensitive and the D-2 polypeptide is still cut, but the D-1 polypeptide is cut only under certain conditions. A protection of the D-1 polypeptide is possible with inhibitors of photosystem II of the DCMU/triazine-type and with an artificial acceptor quinone, but not with inhibitors of the phenol-type. In hexane extracted membranes plastoquinone has been removed from the QB site. Both the D-1 and D-2 polypeptides are more trypsin sensitive in such preparations. The D-1, but not the D-2 polypeptide is protected when plastoquinone has been readded to the membrane before the trypsin digestion.The results show that plastoquinone, artificial quinones and inhibitors of photosystem II at the QB site, but also carotene to a lesser extent, have an effect on the conformation of both the D-1 and D-2 polypeptide. it is postulated that the amino acid sequence around arginine 238 of the D-1 polypeptide is part of the QB binding niche. Furthermore this sequence is modified or its conformation is changed if the QB site is occupied by either plastoquinone or a DCMU-type inhibitor because under these conditions arginine 238 is less accessible to the trypsin. If the QB site, however, is empty, the amino acid sequence with arg 238 is very trypsin sensitive. This property of modulation or the conformation of the amino acid sequence of the D-1 polypeptide by the state of the QB site is likely to be relevant also for the events in the rapid turnover of the D-1 polypeptide.Abbreviations BNT 2-bromo-4-nitro-thymol - DCMU dichlorophenyldimethylurea - PMSF phenylmethylsulfonylfluoride - SDS sodium dodecylsulfate  相似文献   

13.
A detailed comparison of key components in the Photosystem II complexes of higher plants and cyanobacteria was carried out. While the two complexes are overall very similar, significant differences exist in the relative orientation of individual components relative to one another. We compared a three-dimensional map of the inner part of plant PS II at 8 Å resolution, and a 5.5 Å projection map of the same complex determined by electron crystallography, to the recent 3.5–3.8 Å X-ray structures of cyanobacterial complexes. The largest differences were found in the rotational alignment of the cyt b^559 subcomplex, and of the CP47 core antenna with respect to the D1/D2 reaction centre. Within the D1/D2 proteins, there are clear differences between plants and cyanobacteria at the stromal ends of membrane-spanning helices, even though these proteins are highly homologous. Notwithstanding these differences in the protein scaffold, the distances between the critical photosynthetic pigment cofactors seem to be precisely conserved. The different protein arrangements in the two complexes may reflect an adaptation to the two very different antenna systems, membrane-extrinsic phycobilisomes for cyanobacteria, and membrane-embedded chlorophyll a/b proteins in plants.  相似文献   

14.
The fluorescence emission characteristics of the photosynthetic apparatus under conditions of open (F0) and closed (FM) Photosystem II reaction centres have been investigated under steady state conditions and by monitoring the decay lifetimes of the excited state, in vivo, in the green alga Chlorella sorokiniana. The results indicate a marked wavelength dependence of the ratio of the variable fluorescence, FV = FM − F0, over FM, a parameter that is often employed to estimate the maximal quantum efficiency of Photosystem II. The maximal value of the FV/FM ratio is observed between 660 and 680 nm and the minimal in the 690–730 nm region. It is possible to attribute the spectral variation of FV/FM principally to the contribution of Photosystem I fluorescence emission at room temperature. Moreover, the analysis of the excited state lifetime at F0 and FM indicates only a small wavelength dependence of Photosystem II trapping efficiency in vivo.  相似文献   

15.
The location and expression of the previously uncharacterised photosystem II subunit PsbX have been analysed in higher plants. We show that this protein is a component of photosystem II (PSII) core particles but absent from light-harvesting complexes or PSII reaction centres. PsbX is, however, localised to the near vicinity of the reaction centre because it can be cross-linked to cytochrome b559, which is known to be associated with the D1/D2 dimer. We also show that the expression of this protein is tightly regulated by light, since neither protein nor mRNA is found in dark-grown plants.  相似文献   

16.
We have proposed a model for the oligomeric c-rotor of the Fo sector of ATP synthase and its interaction with subunit a during H+-transport driven rotation. The model is based upon the solution structure of monomeric subunit c, determined by NMR, and an extensive series of cross-linking distance constraints between c subunits and between subunits c and a. To explain the complete set of cross-linking data, we have suggested that the second transmembrane helix rotates during its interaction with subunit a in the course of the H+-translocation cycle. The H+-transport coupled rotation of this helix is proposed to drive the stepwise movement of the c-oligomeric rotor. The model is testable and provides a useful framework for addressing questions raised by other experiments.  相似文献   

17.
The FB iron-sulfur cluster is destroyed preferentially by treating Photosystem I complexes with HgCl2(Kojima Y, Niinomi Y, Tsuboi S, Hiyama T and Sakurai H (1987) Bot Mag 100: 243–53). When FB is 95% depleted but FAis quantitatively retained in cyanobacterial PS I complexes, the reduction potential of FA remains highly electronegative (Em=–530 mV, n=1), the EPR spectral and spin relaxation properties of FA and FXremain unchanged, but NADP+ photoreduction rates decline from 552 to 72 mol mg Chl–1 h–1.When FB is reconstituted with FeCl3, Na2S and -mercaptoethanol, NADP+photoreduction rates recover to 528 mol mg Chl–1 h–1. The correlation between the presence of FBand NADP+ photoreduction provides direct experimental evidence that this iron-sulfur cluster is required for electron throughput from cytochromec 6 to flavodoxin or ferredoxin in Photosystem I.Abbreviations Chl chlorophyll - DPIP dichlorophenolindophenol - PS I Photosystem I Published as Journal Series #11091 of the University of Nebraska Agricultural Research Division. This paper is dedicated to the memory of the late Professor Daniel Arnon, who is remembered for his gracious and generous encouragement of the senior author's early career.  相似文献   

18.
Photosystem I is a large macromolecular complex located in the thylakoid membranes of chloroplasts and in cyanobacteria that catalyses the light driven reduction of ferredoxin and oxidation of plastocyanin. Due to the very negative redox potential of the primary electron transfer cofactors accepting electrons, direct estimation by redox titration of the energetics of the system is hampered. However, the rates of electron transfer reactions are related to the thermodynamic properties of the system. Hence, several spectroscopic and biochemical techniques have been employed, in combination with the classical Marcus theory for electron transfer tunnelling, in order to access these parameters. Nevertheless, the values which have been presented are very variable. In particular, for the case of the tightly bound phylloquinone molecule A1, the values of the redox potentials reported in the literature vary over a range of about 350 mV. Previous models of Photosystem I have assumed a unidirectional electron transfer model. In the present study, experimental evidence obtained by means of time resolved absorption, photovoltage, and electron paramagnetic resonance measurements are reviewed and analysed in terms of a bi-directional kinetic model for electron transfer reactions. This model takes into consideration the thermodynamic equilibrium between the iron-sulfur centre FX and the phylloquinone bound to either the PsaA (A1A) or the PsaB (A1B) subunit of the reaction centre and the equilibrium between the iron-sulfur centres FA and FB. The experimentally determined decay lifetimes in the range of sub-picosecond to the microsecond time domains can be satisfactorily simulated, taking into consideration the edge-to-edge distances between redox cofactors and driving forces reported in the literature. The only exception to this general behaviour is the case of phylloquinone (A1) reoxidation. In order to describe the reported rates of the biphasic decay, of about 20 and 200 ns, associated with this electron transfer step, the redox potentials of the quinones are estimated to be almost isoenergetic with that of the iron sulfur centre FX. A driving force in the range of 5 to 15 meV is estimated for these reactions, being slightly exergonic in the case of the A1B quinone and slightly endergonic, in the case of the A1A quinone. The simulation presented in this analysis not only describes the kinetic data obtained for the wild type samples at room temperature and is consistent with estimates of activation energy by the analysis of temperature dependence, but can also explain the effect of the mutations around the PsaB quinone binding pocket. A model of the overall energetics of the system is derived, which suggests that the only substantially irreversible electron transfer reactions are the reoxidation of A0 on both electron transfer branches and the reduction of FA by FX.  相似文献   

19.
Visible absorption spectra and circular dichroism (CD) of the red absorption band of isolated photosystem II reaction centers were measured at room temperature during progressive bleaching by electrochemical oxidation, in comparison with aerobic photochemical destruction, and with anaerobic photooxidation in the presence of the artificial electron acceptor silicomolybdate. Initially, selective bleaching of peripheral chlorophylls absorbing at 672 nm was obtained by electrochemical oxidation at +0.9 V, whereas little selectivity was observed at higher potentials. Illumination in the presence of silicomolybdate did not cause a bleaching but a spectral broadening of the 672-nm band was observed, apparently in response to the oxidation of carotene. The 672-nm absorption band is shown to exhibit a positive CD, which accounts for the 674-nm shoulder in CD spectra at low temperature. The origin of this CD is discussed in view of the observation that all CD disappears with the 680-nm absorption band during aerobic photodestruction.  相似文献   

20.
Accessory chlorophylls (B(A/B)) in bacterial photosynthetic reaction center play a key role in charge-separation. Although light-exposed and dark-adapted bRC crystal structures are virtually identical, the calculated B(A) redox potentials for one-electron reduction differ. This can be traced back to different orientations of the B(A) ester-group. This tuning ability of chlorophyll redox potentials modulates the electron transfer from SP* to B(A).  相似文献   

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