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1.
Zhang Haoming Yamamoto Yasusi Ishikawa Yasuo Zhang Weila Fischer Gad Wydrzynski Tom 《Photosynthesis research》1997,52(3):215-223
Degradation of the reaction center-binding protein D1 of Photosystem II (PS II) during photoinhibition is dependent on the action of active oxygen species and/or D1-specific proteases. Protein conformational changes may be involved in the process of D1 degradation. In the present study, we determined the effect of H2O2 on spinach PS II-enriched membranes and core complexes with respect to electron transport, Mn content and protein secondary structural changes as measured by Fourier transform infrared (FTIR) spectroscopy. H2O2 is effective in removing catalytic Mn in PS II, especially in PS II core complexes depleted of OEC18 and OEC24, impairing the donor-side. By quantitative analysis of the amide I band (1600 – 1700 cm-1) with both aqueous and dehydrated PS II samples, we found that no significant secondary structural changes are associated with H2O2 treatment in the dark, even though there is some cleavage of the D1 protein by H2O2 treatment as determined by Western analysis with specific antibodies. In contrast, a large decrease in the -helices in the PS II core occurs, with or without H2O2 treatment, after 20 min strong illumination and there is more extensive degradation of the D1 protein. Our results suggest that high light enhances the cleavage of the D1 protein which is reflected in the large protein secondary structural changes in PS II detected by FTIR measurements. 相似文献
2.
Target theory and the photoinactivation of Photosystem II 总被引:1,自引:0,他引:1
Application of target theory to the photoinactivation of Photosystem II in pea leaf discs (Park et al. 1995, 1996a,b) reveals that there is a critical light dosage below which there is complete photoprotection and above which there is photoinactivation (i.e a light-induced loss of oxygen flash yield). The critical dosage is about 3 mol photons m–2 for medium and high light-grown leaves and 0.36 mol photons m–2 for low light-grown leaves. Photoinactivation is a one-hit process with an effective cross-section of 0.045 m2 mol–1 photons which does not vary with growth irradiance, unlike the cross-section for oxygen evolution which increases with decreasing growth irradiance. The cross-section for oxygen evolution increased by about 20% following exposure to 6.8 mol photons m–2 which may be due to energy transfer from photoinactivated units to functional Photosystem II units. We propose that the photoinactivation of PS II begins when a small group of PS II pigment molecules whose structure is uninfluenced by growth irradiance, becomes uncoupled energetically from the rest of the photosynthetic unit and thus no longer transfers excitions to P680. De-excitation of this group of pigment molecules provides the energy which leads to the damage of Photosystem II. Treatment of pea leaves with dithiothreitol, an inhibitor of the xanthophyll cycle, decreases the critical dosage i.e. decreases photoprotection but has no effect on the PS II photoinactivation cross-section. Treatment with 1 M nigericin increased the photoinactivation cross-section of PS II as did exposure to lincomycin which inhibits D1 protein synthesis and thus the repair of PS II reaction centres.Abbreviations DTT-
dithiothreitol
- PS II-
Photosystem II
- Fm-
maximum fluorescence
- Fv-
variable fluorescence
- LHCIIb-
main light harvesting pigment-protein complex of PS II
- D1 protein-
psbA gene product
- P680-
reaction centre chlorophyll of Photosystem II
- Qa-
first quinone electron acceptor of Photosystem II
- (o2)-
cross-section for oxygen evolution
- (pi)-
cross-section for photoinactivation 相似文献
3.
Certain phenolic compounds represent a distinct class of Photosystem (PS) II QB site inhibitors. In this paper, we report a detailed study of the effects of 2,4,6-trinitrophenol (TNP) and other phenolic inhibitors, bromoxynil and dinoseb, on PS II energetics. In intact PS II, phenolic inhibitors bound to only 90-95% of QB sites even at saturating concentrations. The remaining PS II reaction centers (5-10%) showed modified QA to QB electron transfer but were sensitive to urea/triazine inhibitors. The binding of phenolic inhibitors was 30- to 300-fold slower than the urea/triazine class of QB site inhibitors, DCMU and atrazine. In the sensitive centers, the S2QA− state was 10-fold less stable in the presence of phenolic inhibitors than the urea/triazine herbicides. In addition, the binding affinity of phenolic herbicides was decreased 10-fold in the S2QA− state than the S1QA state. However, removal of the oxygen-evolving complex (OEC) and associated extrinsic polypeptides by hydroxylamine (HA) washing abolished the slow binding kinetics as well as the destabilizing effects on the charge-separated state. The S2-multiline electron paramagnetic resonance (EPR) signal and the ‘split’ EPR signal, originating from the S2YZ state showed no significant changes upon binding of phenolic inhibitors at the QB site. We thus propose a working model where QA redox potential is lowered by short-range conformational changes induced by phenolic inhibitor binding at the QB niche. Long-range effects of HA-washing eliminate this interaction, possibly by allowing more flexibility in the QB site. 相似文献
4.
A set of Mn K-edge XANES spectra due to the redox states S0–S3 of the OEC were determined by constructing a highly-sensitive X-ray detection system for use with physiologically native PS II membranes capable of cycling under a series of saturating laser-flashes. The spectra showed almost parallel upshifts with relatively high K-edge half-height energies given by 6550.9±0.2 eV, 6551.7±0.2 eV, 6552.5±0.2 eV and 6553.6±0.2 eV for the S0, S1, S2 and S3 states, respectively. The successive difference spectra between S0 and S1, S1 and S2, and S2 and S3 states were found to exhibit a similar peak around 6552–6553 eV, indicating that one Mn(III) ion or its direct ligand is univalently oxidized upon each individual S-state transition from S0 to S3. The present data, together with other observations of EPR and pre-edge XANES spectroscopy, suggest that the oxidation state of the Mn cluster undergoes a periodic change; S0: Mn(III,III,III,IV) S1: Mn(III,IV,III,IV) S2: Mn(III,IV,IV,IV) S3: Mn(IV,IV,IV,IV) or Mn(III,IV,IV,IV)·L+ with L being a direct ligand of a Mn(III) ion.Abbreviations Chl
chlorophyll
- D
tyrosine 160 on the D2 protein, an accessory electron donor in PS II
- D+
the oxidized form of D
- EDTA
ethylene-diaminetetraacetic acid
- EPR
electron paramagnetic resonance
- EXAFS
extended X-ray absorption fine structure
- HL
py-2,6-bis[bis(2-pyridylmethyl)aminomethyl]-4-methylphenol
- Mes
2-(N-morpholino)ethanesulfonic acid
- N4
py-tris(2-pyridylmethyl)amine
- OEC
oxygen evolving complex
- P680
primary electron donor of PS II
- PS II
Photosystem II
- Q400
a high spin Fe3+ of the iron-quinone acceptor complex in PS II
- SSD
solid state detector
- XAFS
X-ray absorption fine structure
- XANES
X-ray absorption near edge structure 相似文献
5.
Vyacheslav Klimov Gennady Ananyev Olga Zastryzhnaya Tom Wydrzynski Gernot Renger 《Photosynthesis research》1993,38(3):409-416
The present study describes the formation of different forms of peroxide in Photosystem II (PS II) by using a chemiluminescence detection technique. Four chemiluminescence signals (A, B, C and D) of the luminolperoxidase (Lu-Per) system, which detects peroxide, are found in illuminated O2-evolving Photosystem II (PS II) membrane fragments isolated from spinach. Signal A (free peroxide) peaking around 0.2–0.3 s after mixing PS II membrane fragments with Lu-Per is eliminated by catalase or removal of oxygen from the suspension and ascribed to O2 interaction with reduced PS II electron acceptors. In contrast, signal B peaking around 1.5 min remains largely unaffected under anaerobic conditions, as well as in the presence of catalase (20 g/ml). Under flash illumination the extent of this signal exhibits a weak period four oscillation (maximum at third and 7th flash). Its yield increases up to the third flash, but is close to zero in the fourth flash. An analogous behaviour is observed in flashes 5 to 8. Signal B is ascribed to Lu-Per interaction with the water-oxidizing system being in S2 and/or S3-state. Signal C (bound peroxide) detected as free peroxide after acid decomposition of illuminated PS II particles is observed on the 1 st flash and oscillates with period 2 with superposition of period 4. It is evidently related to peroxide either released from S2 or formed at S2 upon acid shock treatment. Signal D (slowly released peroxide) peaking around 2–3 s after mixing is observed in samples after various treatments (LCC-incubation, washing with 1 M NaCl at pH 8 or with 1 M CaCl2, Cl--depletion) that lead to at least partial removal of the extrinsic proteins of 18, 24 and 33 kDa without Mn extraction. The average amplitude of this signal corresponds with a yield of about 0.2 H2O2 molecules per RC and flash. In a flash train, the extent of signal D exhibits an oscillation pattern with a minimum at the 3rd flash. We assume that these treatments increase the release of bound peroxide (upon injection into the Lu-Per assay) either formed in the normal oxidative pathway of the water oxidase in the S2 or the S3-state or give rise to peroxide formation due to higher accessibility of the Mn-cluster to water molecules.Abbreviations DCPIP
2,6-dichlorophenolindophenol
- DPC
diphenylcarbazide
- LCC
lauroylcholine chloride
- Lu-Per
luminol peroxidase
- PS II
Photosystem II
- RC
reaction center
- S2, S3
redox states of the water oxidizing system
- TEMED-N,N,N,N
tetramethylethylenediamine 相似文献
6.
Old and very recent experiments on the extent and the rate of proton release during the four reaction steps of photosynthetic water oxidation are reviewed. Proton release is discussed in terms of three main sources, namely the chemical production upon electron abstraction from water, protolytic reactions of Mn-ligands (e.g. oxo-bridges), and electrostatic response of neighboring amino acids. The extent of proton release differs between the four oxidation steps and greatly varies as a function of pH both, but differently, in thylakoids and PS II-membranes. Contrastingly, it is about constant in PS II-core particles. In any preparation, and on most if not all reaction steps, a large portion of proton transfer can occur very rapidly (<20 s) and before the oxidation of the Mn-cluster by Yz
+ is completed. By these electrostatically driven reactions the catalytic center accumulates bases. An additional slow phase is observed during the oxygen evolving step, S3S4S0. Depending on pH, this phase consists of a release or an uptake of protons which accounts for the balance between the number of preformed bases and the four chemically produced protons. These data are compatible with the hypothesis of concerted electron/proton-transfer to overcome the kinetic and energetic constraints of water oxidation.Abbreviations BBY-membranes
Photosystem II-enriched membrane fragments prepared after Berthold, Babcock and Yocum (1981)
- BSA
bovine serum albumin
- Chl
chlorophyll
- CAB-protein
chlorophyll a/b-binding protein
- core particles
oxygen evolving reaction center core particles of Photosystem II
- Cyt
cytochrome
- DCBQ
2,5-dichloro-p-benzoquinone
- IML
intermittent light
- P-680
primary electron donor of Photosystem II
- PS II
Photosystem II
- Yz
tyrosine residue on the D1 polypeptide, electron carrier between manganese and P-680
- photochemical reaction
相似文献
7.
The anion azide, N3
-, has been previously found to be an inhibitor of oxygen evolution by Photosystem II (PS II) of higher plants. With respect to chloride activation, azide acts primarily as a competitive inhibitor but uncompetitive inhibition also occurs [Haddy A, Hatchell JA, Kimel RA and Thomas R (1999) Biochemistry 38: 6104–6110]. In this study, the effects of azide on PS II-enriched thylakoid membranes were characterized by electron paramagnetic resonance (EPR) spectroscopy. Azide showed two distinguishable effects on the S2 state EPR signals. In the presence of chloride, which prevented competitive binding, azide suppressed the formation of the multiline and g = 4.1 signals concurrently, indicating that the normal S2 state was not reached. Signal suppression showed an azide concentration dependence that correlated with the fraction of PS II centers calculated to bind azide at the uncompetitive site, based on the previously determined inhibition constant. No evidence was found for an effect of azide on the Fe(II)QA
- signals at the concentrations used. This result is consistent with placement of the uncompetitive site on the donor side of PS II as suggested in the previous study. In chloride-depleted PS II-enriched membranes azide and fluoride showed similar effects on the S2 state EPR signals, including a notable increase and narrowing of the g = 4.1 signal. Comparable effects of other anions have been described previously and apparently take place through the chloride-competitive site. The two azide binding sites described here correlate with the results of other studies of Lewis base inhibitors.This revised version was published online in October 2005 with corrections to the Cover Date. 相似文献
8.
The functional size of Photosystem II (PS II) was investigated by radiation inactivation. The technique provides an estimate of the functional mass required for a specific reaction and depends on irradiating samples with high energy -rays and assaying the remaining activity. The analysis is based on target theory that has been modified to take into account the temperature dependence of radiation inactivation of proteins. Using PS II enriched membranes isolated from spinach we determined the functional size of primary charge separation coupled to water oxidation and quinone reduction at the QB site: H2O (Mn)4 Yz P680 Pheophytin Q phenyl-p-benzoquinone. Radiation inactivation analysis indicates a functional mass of 88 ± 12 kDa for electron transfer from water to phenyl-p-benzoquinone. It is likely that the reaction center heterodimer polypeptides, D1 and D2, contribute approximately 70 kDa to the functional mass, in which case polypeptides adding up to approximately 20 kDa remain to be identified. Likely candidates are the and subunits of cytochrome b
559and the 4.5 kDa psbI gene product.Abbreviations Cyt
cytochrome
- PS
Photosystem
- P680
primary electron donor of Photosystem II
- QA
primary quinone acceptor of Photosystem II
- QB
secondary quinone acceptor of Photosystem II
- Yz
tyrosine donor to P680 相似文献
9.
Jonathan H. A. Nugent Dugald J. Maclachlan Stephen E. J. Rigby Michael C. W. Evans 《Photosynthesis research》1993,38(3):341-346
Our recent EPR and EXAFS experiments investigating the structure of the oxygen-evolving complex of PS II are discussed. PS II treatments which affect the cofactors calcium and chloride have been used to poise samples in modified forms of the S-states, S1, S2 and S3. X-ray absorption studies indicate a similar overall structure for the manganese complex between treated and native samples although the influence of the treatments and cofactors is observed. Manganese oxidation (or oxidation of a ligand to the manganese cluster) is indicated to occur on each of the transitions S1 S2 and S2 S3 in these modified samples. The cluster appears to contain at least two inequivalent Mn-Mn pairs. In the native samples the Mn-Mn distance is 2.7 Å, but in samples where the calcium site is affected, one of the pairs has a 3.0 Å Mn-Mn distance. The intensity of the 3.3/3.6 Å interaction is reduced on sodium chloride treatment (calcium depletion) perhaps indicating calcium binding close to the manganese cluster. From EPR data we also propose that treatments which affect calcium and chloride binding cause a modification of the native S2 state, slow the reduction of Yz
and allow an S3 EPR signal to be observed following illumination. The origin of the S3 EPR signal, a modified S3 or S2 X where X is an organic radical of unknown charge, is discussed in relation to the results from the EXAFS studies.Abbreviations EPR
electron paramagnetic resonance spectroscopy
- EXAFS
extended X-ray absorption fine structure
- HTG
n-heptyl -d-thioglucoside
- MES
2(N-morpholino)ethanesulfonic acid
- OEC
oxygen evolving complex
- PPBQ
phenyl-1,4-benzoquinone
- PS II
Photosystem II
- Yz
redox active tyrosine 相似文献
10.
Redox changes of the oxygen evolving complex in PS II core particles were investigated by absorbance difference spectroscopy in the UV-region. The oscillation of the absorbance changes induced by a series of saturating flashes could not be explained by the minimal Kok model (Kok et al. 1970) consisting of a 4-step redox cycle, S0 S1 S2 S3 S0, although the values of most of the relevant parameters had been determined experimentally. Additional assumptions which allow a consistent fit of all data are a slow equilibration of the S3 state with an inactive state, perhaps related to Ca2+-release, and a low quantum efficiency for the first turnover after dark-adaptation. Difference spectra of the successive S-state transitions were determined. At wavelengths above 370 nm, they were very different due to the different contribution of a Chl bandshift in each spectrum. At shorter wavelengths, the S1 S2 transition showed a difference spectrum similar to that reported by Dekker et al. 1984b and attributed to an Mn(III) to Mn(IV) oxidation. The spectrum of absorbance changes associated with the S2 S3 transition was similar to that reported by Lavergne 1991 for PS II membranes. The S0 S1 transition was associated with a smaller but still substantial absorbance increase in the UV. Differences with the spectra reported by Lavergne 1991 are attributed to electrostatic effects on electron transfer at the acceptor side associated with the S-state dependence of proton release in PS II membranes.Abbreviations Bis-Tris
(bis[2-hydroxyethyl]imino-tris[hydroxymethyl]methane)
- DCBQ
2,5-dichloro-p-benzoquinone
- DCMU
3-(3,4-dichlorophenyl)-1,1-dimethylurea
- PS II
Photosystem II
- QA
secondary electron acceptor of PS II
- S0 to S4
redox state of the oxygen evolving complex
- Z
secondary electron donor of PS II 相似文献
11.
Treatment of Photosystem II (PS II) with low concentrations of hydroxylamine is known to cause a two-flash delay in the O2-evolution pattern, and in the formation of the S2-state multiline EPR signal, due to the two-electron reduction of the S1-state by hydroxylamine to form the S-1-state. Past work has shown that these delays are not reversed by washing out the hydroxylamine nor by adding DCBQ or ferricyanide to oxidize the residual hydroxylamine, but are reversed by illumination with two saturating flashes followed by a 30-min dark incubation. We have examined the effects of treatments aimed at restoring the normal flash-induced O2-evolution pattern and S2-state multiline EPR signal after treatment of PS II with 40 M hydroxylamine. In agreement with past work, we find that the two-flash delay in O2 evolution is not reversed when the hydroxylamine is removed by three cycles of centrifugation and resuspension in hydroxylamine-free buffer nor by adding ferricyanide or DCBQ to oxidize the unreacted hydroxylamine. However, the normal flash-induced O2-evolution pattern is restored by illumination with two saturating flashes followed by a 30-min dark incubation (after the sample was first treated with 40 M hydroxylamine and the unreacted hydroxylamine was removed); illumination with one saturating flash followed by a 30-min dark incubation is only partially effective. These results show that ferricyanide and DCBQ are not effective at oxidizing the S-1-state to the S1-state. In contrast, adding hypochlorite (OCl-) after treatment with hydroxylamine restored the normal flash-induced O2-evolution pattern and also restored the formation of the S2-state multiline EPR signal by illumination at 200 K. We conclude that hypochlorite is capable of oxidizing the S-1-state to the S1-state. This is the first example of a chemical treatment that advances the delayed flash-induced O2 evolution pattern.Abbreviations DCBQ
2,5-dichloro-p-benzoquinone
- OEC
O2-evolving center 相似文献
12.
We have measured, under Cu (II) toxicity conditions, the oxygen-evolving capacity of spinach PS II particles in the Hill reactions H2OSiMo (in the presence and absence of DCMU) and H2OPPBQ, as well as the fluorescence induction curve of Tris-washed spinach PS II particles. Cu (II) inhibits both Hill reactions and, in the first case, the DCMU-insensitive H2O SiMo activity. In addition, the variable fluorescence is lowered by Cu (II). We have interpreted our results in terms of a donor side inhibition close to the reaction center. The same polarographic and fluorescence measurements carried out at different pHs indicate that Cu (II) could bind to amino acid residues that can be protonated and deprotonated. In order to reverse the Cu (II) inhibition by a posterior EDTA treatment, in experiments of preincubation of PS II particles with Cu (II) in light we have demonstrated that light is essential for the damage due to Cu (II) and that this furthermore is irreversible.Abbreviations DCMU
3-(3,4-dichlorophenyl)-1, 1-dimethyl urea
- DCIP
2,6-dichlorophenolindophenol
- DPC
1,5-diphenilcarbazide
- Fo
initial non-variable fluorescence
- FI
intermediate fluorescence yield
- Fm
maximum fluorescence yield
- Fv
variable fluorescence yield
- Mes
2,-(N-morpholino)ethanosulfonic acid
- OEC
oxygen-evolving complex
- P680
Primary electron donor chlorophyll
- Pheo
pheophytin
- PPBQ
phenyl-p-benzo-quinone
- PS II
Photosystem II
- SiMo
Silicomolybdate
- QB
secondary quinone acceptor
- QA
primary quinone aceptor
- Tris
N-tris(hydroxymethyl)amino ethane
- Tyrz
electron carrier functioning between P680 and the Mn cluster
This article is dedicated to Prof. Dr. Harmut Lichtenthaler on the occasion of his 60th birthday. 相似文献
13.
In recent years Photosystem II, and in particular the oxygen evolving component of the enzyme, have been the subject of intense biochemical and biophysical analysis. To date no high resolution structural model of the complex has been produced. As a consequence unambiguous interpretation of much experimental data has proven difficult, leading to a lack of consensus over many basic questions regarding the mechanisms involved, the oligomerization state of the enzyme in vivo and even the exact biochemical composition.This review is a summary of the progress towards the production of a structural model of PS II-derived from either X-ray crystallography or electron microscopy based techniques-and the current opinions, which have arisen from these structural analyses, on the structural topology and assemblage of the various subunits that constitute the complex.Abbreviations C12-M
dodecyl maltoside
- CP
chlorophyll protein
- cyt b-559
cytochrome b-559
- DMPC
dimyristoyl phosphatidyl choline
- EC
electron crystallography
- EM
electron microscopy
- LHC II
light harvesting complex II
- OEC
oxygen evolving complex
- OG
octyl--glucopyranoside
- PS I
Photosystem I
- PS II
Photosystem II
- Tris
N-tris (hydroxymethyl) amino ethane 相似文献
14.
Chemeris Yu. K. Korolkov N. S. Seifullina N. Kh. Rubin A. B. 《Russian Journal of Plant Physiology》2004,51(5):584-589
Incubation of green alga Chlorella pyrenoidosa Chick in darkness at 37–38°C for 10–30 h resulted in inactivation of the oxygen-evolving complex (OEC): the maximum yield of oxygen evolution during a series of short light flashes shifted from the third to the fifth flash; the transition of S2- and S3-states of OEC to a stable S1-state was markedly accelerated. This inactivation of OEC was accompanied by the accumulation of inactive complexes of photosystem II (PSII), in which the reduction of primary quinone acceptor and the conversion into the closed state occurred with a low efficiency, even in the presence of 5 M DCMU. The treatment of light-grown algal cells with hydroxylamine impaired OEC functioning, in similarity to the effect of dark incubation, but caused no accumulation of inactive PSII complexes. We conclude that the inactivation of OEC is not the cause of the inactivation of PSII complex. The decline in the efficiency of electron-transport reactions, both on the donor and acceptor sides of PSII may be related to modification of major proteins in the PS II reaction center. 相似文献
15.
An overview is presented of secondary electron transfer at the electron donor side of Photosystem II, at which ultimately two water molecules are oxidized to molecular oxygen, and the central role of manganese in catalyzing this process is discussed. A powerful technique for the analysis of manganese redox changes in the water-oxidizing mechanism is the measurement of ultraviolet absorbance changes, induced by single-turnover light flashes on dark-adapted PS II preparations. Various interpretations of these ultraviolet absorbance changes have been proposed. Here it is shown that these changes are due to a single spectral component, which presumably is caused by the oxidation of Mn(III) to Mn(IV), and which oscillates with a sequence +1, +1, +1, –3 during the so-called S0 S1 S2 S3 S0 redox transitions of the oxygen-evolving complex. This interpretation seems to be consistent with the results obtained with other techniques, such as those on the multiline EPR signal, the intervalence Mn(III)-Mn(IV) transition in the infrared, and EXAFS studies. The dark distribution of the S states and its modification by high pH and by the addition of low concentrations of certain water analogues are discussed. Finally, the patterns of proton release and of electrochromic absorbance changes, possibly reflecting the change of charge in the oxygen-evolving system, are discussed. It is concluded that nonstoichiometric patterns must be considered, and that the net electrical charge of the system probably is the highest in state S2 and the lowest in state S1. 相似文献
16.
In this communication, we report our progress on the development of low-frequency Fourier transform infrared (FTIR) spectroscopic
techniques to study metal-substrate and metal-ligand vibrational modes in the Photosystem II/oxygen-evolving complex (PS II/OEC).
This information will provide important structural and mechanistic insight into the OEC. Strong water absorption in the low-frequency
region (below 1000 cm−1), a lack of suitable materials, and temperature control problems have limited previous FTIR spectroscopic studies of the
OEC to higher frequencies (>1000 cm−1). We have overcome these technical difficulties that have blocked access to the low-frequency region and have developed successive
instruments that allow us to move deeper into the low-frequency region (down to 350 cm−1), while increasing both data accumulation efficiency and S/N ratio. We have detected several low-frequency modes in the S2/S1spectrum that are specifically associated with these two states. Our results demonstrate the utility of FTIR techniques in
accessing low-frequency modes in Photosystem II and in proteins generally.
This revised version was published online in June 2006 with corrections to the Cover Date. 相似文献
17.
An abnormal, structurally modified, kinetically stable S2-state has been reported to be induced when Photosystem II was treated with NaCl-EGTA (or EDTA) in the light or with pH in darkness, both are assumed to release functional Ca2+. In order to compare the mechanism of induction of modified S2-state between the two treatments, effects of illumination during or before low pH-treatment on formation of the abnormal S2-state were investigated by means of thermoluminescence measurements and low temperature EPR spectroscopy. Following results have been obtained: Flash illumination during low pH-treatment did not practically induce the abnormal S2-state, whereas preflash illumination given immediately before low pH-treatment efficiently induced the abnormal S2-state, and its amplitude showed a period-four oscillation on varying the preflash number with maxima at the second and sixth flashes. The abnormal S2-state thus induced by preflashes was identical with the modified S2-state that could be induced in dark-low pH-treated Photosystem II by excitation at 0°C after neutralization to pH 6.5. It was inferred that in low pH-treatment, modified S2-state can be formed from both S2- and S3-states, but its yield from the latter is much higher than from the former, consistent with the early results by Boussac et al. obtained for NaCl-EGTA-light or NaCl-citrate-light treatment.Abbreviations DCMU
3-(3,4-dichlorophenyl)-1,1-dimethylurea
- EDTA
ethylenediaminetetraactate
- EGTA
ethylene glycol bis(-aminoethylether)-N,N,N,N-tetraacetic acid
- Mes
2-(N-morpholino)ethanesulfonic acid
- PS II
Photosystem II 相似文献
18.
Svetlana M. Kochubey Victor V. Shevchenko Olga I. Volovik 《Photosynthesis research》1993,38(2):153-157
Chloroplast proteins were phosphorylated under two test conditions: white light irradiance alone and white light irradiance with the addition of glucose and glucose oxidase, used to produce an anaerobic medium. The interaction of phospho-LHC II with Photosystem 1 (PS 1) was studied for two types of PS I preparation. Changes in the chlorophyll a/b ratio and the ratio of 650 and 680 nm band intensities (E650/E680) in fluorescence excitation spectra were used in calculating the phospho-LHC II portion which became associated with PS 1. It is shown that the associated portion of phospho-LHC II varies for each of the PS 1 preparations and phosphorylation procedures. Possible conclusions as regards the transfer of various sets of LHC II subpopulations under different phosphorylation procedures and the differences of interaction with PS 1 are discussed.Abbreviations PS 1
Photosystem 1
- PS 2
Photosystem 2
- LHC II
light-harvesting chlorophyll a/b protein complex II
- Chl
chlorophyll
-
fluorescence quantum yield
- f
life time of fluorescence at =685 nm
- F735
fluorescence band with a maximum at 735 nm
- F685
fluorescence band with a maximum at 685 nm
- E650/E680
ratio of amplitudes in excitation fluorescence spectrum at 650 and 680 nm 相似文献
19.
Curtis W. Hoganson Demetrios F. Ghanotakis Gerald T. Babcock Charles F. Yocum 《Photosynthesis research》1989,22(3):285-293
Manganese in the oxygen-evolving complex is a physiological electron donor to Photosystem II. PS II depleted of manganese may oxidize exogenous reductants including benzidine and Mn2+. Using flash photolysis with electron spin resonance detection, we examined the room-temperature reaction kinetics of these reductants with Yz
+, the tyrosine radical formed in PS II membranes under illumination. Kinetics were measured with membranes that did or did not contain the 33 kDa extrinsic polypeptide of PS II, whose presence had no effect on the reaction kinetics with either reductant. The rate of Yz
+ reduction by benzidine was a linear function of benzidine concentration. The rate of Yz
+ reduction by Mn2+ at pH 6 increased linearly at low Mn2+ concentrations and reached a maximum at the Mn2+ concentrations equal to several times the reaction center concentration. The rate was inhibited by K+, Ca2+ and Mg2+. These data are described by a model in which negative charge on the membrane causes a local increase in the cation concentration. The rate of Yz
+ reduction at pH 7.5 was biphasic with a fast 400 s phase that suggests binding of Mn2+ near Yz
+ at a site that may be one of the native manganese binding sites.Abbreviations PS II
Photosystem II
- YD
tyrosine residue in Photosystem II that gives rise to the stable Signal II EPR spectrum
- Yz
tyrosine residue in Photosystem II that mediates electron transfer between the reaction center chlorophyll and the site of water oxidation
- ESR
electron spin resonance
- DPC
diphenylcarbazide
- DCIP
dichlorophenolindophenol 相似文献
20.
Ondrej Prasil Zbigniew Kolber Joseph A. Berry Paul G. Falkowski 《Photosynthesis research》1996,48(3):395-410
The oxygen flash yield (YO2) and photochemical yield of PS II (PS II) were simultaneously detected in intact Chlorella cells on a bare platinum oxygen rate electrode. The two yields were measured as a function of background irradiance in the steady-state and following a transition from light to darkness. During steady-state illumination at moderate irradiance levels, YO2 and PS II followed each other, suggesting a close coupling between the oxidation of water and QA reduction (Falkowski et al. (1988) Biochim. Biophys. Acta 933: 432–443). Following a light-to-dark transition, however, the relationship between QA reduction and the fraction of PS II reaction centers capable of evolving O2 became temporarily uncoupled. PS II recovered to the preillumination levels within 5–10 s, while the YO2 required up to 60 s to recover under aerobic conditions. The recovery of YO2 was independent of the redox state of QA, but was accompanied by a 30% increase in the functional absorption cross-section of PS II (PS II). The hysteresis between YO2 and the reduction of QA during the light-to-dark transition was dependent upon the reduction level of the plastoquinone pool and does not appear to be due to a direct radiative charge back-reaction, but rather is a consequence of a transient cyclic electron flow around PS II. The cycle is engaged in vivo only when the plastoquinone pool is reduced. Hence, the plastoquinone pool can act as a clutch that disconnects the oxygen evolution from photochemical charge separation in PS II.Abbreviations ADRY
acceleration of the deactivation reactions of the water-splitting enzyme (agents)
- Chl
chlorophyll
- cyt
cytochrome
- DCMU
3-(3,4-dichlorophenyl)-1,1-dimethylurea
- FO
minimum fluorescence yield in the dark-adapted state
- FI
minimum fluorescence yield under ambient irradiance or during transition from the light-adapted state
- FM
maximum fluorescence yield in the dark-adapted state
- FM
maximum fluorescence yield under ambient irradiance or during transition from light-adapted state
- FV, FV
variable fluorescence (FV=FM–FO ; FV=FM–FI)
- FRR
fast repetition rate (fluorometer)
- PS II
quantum yield of QA reduction (PS II=(FM – FO)/FM or PS II)=(FM= – FI=)/FM=)
- LHCII
Chl a/b light harvesting complexes of Photosystem II
- OEC
oxygen evolving complex of PS II
- P680
reaction center chlorophyll of PS II
- PQ
plastoquinone
- POH2
plastoquinol
- PS I
Photosystem I
- PS II
Photosystem II
- RC II
reaction centers of Photosystem II
- PS II
the effective absorption cross-section of PHotosystem II
- TL
thermoluminescence
- YO2
oxygen flash yield
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