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1.
Treatment of oxygen-evolving Photosystem II complexes, whichlack light-harvesting chlorophyll a/b proteins, with a seriesof disuccinimidyl esters with different chain lengths yieldeda crosslinked product which consisted of one molecule each ofthe extrinsic 33 kDa and 23 kDa proteins. In addition, crosslinkingbetween the 33 kDa protein and the chlorophyll-carrying 47 kDaprotein and between the 23 kDa and 17 kDa proteins was confirmed.Thus, the three extrinsic proteins are closely associated witheach other to form a complex which is attached to the PS IIreaction center complexes. (Received December 1, 1989; Accepted May 2, 1990)  相似文献   

2.
Reduction kinetics of chloro- or methyl-substituted benzoquinones(BQs) in spinach PSII membrane fragments or n-heptyl-rß-D-thioglucoside-extractedPSII core complexes (HTG-PSII) was studied and compared to thatin cyanobacterial PSII core complexes [Satoh et al. (1995) PlantCell Physiol. 36: 597]. It was found that the BQs accept electronsat two sites (the QB and PQ sites) in the both spinach preparationsas in the cyanobacterial preparation. Maximum turnover rates(Vmax) and binding affinities (Km) of the two sites were estimated.Comparison of the values in PSII membrane fragments with thosein HTG-PSII showed that removal of the membrane structure orlight-harvesting chlorophyll a/b protein complexes from thePSII core complexes had little effect on the characteristicsof the QB site, indicating that the HTG-PSII have the intactQB site and are good materials to study the site. The Km andVmax values were comparable to those in the cyanobacterial preparation. Low affinity (high Km values) and high Vmax values of methyl-substitutedBQs to the QB site and almost the same rate of intrinsic electronflow through the QB site in the both spinach preparations furthersupport the hypothesis that the plastoquinone (PQ) moleculeat the QB site is not replaced by another PQ molecule but, afterreduction, only its head group goes out of the QB pocket, andcomes back after transferring the electrons and protons to afree PQ molecule [Satoh et al. (1993) Z. Naturforsch. 48c: 174]. (Received May 2, 1996; Accepted July 26, 1996)  相似文献   

3.
Stabilities of iron-sulfur centers and reaction center chlorophyllP-700 in Photosystem I reaction center complex (CP1-a), isolatedby sodium dodecyl sulfate treatment from the thermophilic cyanobacteriumSynechococcus elongatus, were studied by EPR and optical spectroscopy.P-700 was destroyed by treatment at temperatures above 80?Cfor 5 minutes with a half inactivation temperature of 93?C.The three iron-sulfur centers FA, FB and FX showed similar thermalstabilities and were half inactivated at about 70?C. Thus, theisolated Photosystem I reaction center complexes of S. elongatusare still highly resistant to heat. (Received May 9, 1990; Accepted June 25, 1990)  相似文献   

4.
Stability of thylakoid components under supra-high irradiancewas studied with the cyanophyte Synechocystis PCC 6714. Theactivity of overall photosynthesis was quickly inactivated (T1/2=20min) under supra-high irradiance (300 W m–2, white light).In parallel with the inactivation of photosynthesis, QA in PSII was also inactivated. Both inactivations were acceleratedby chloramphenicol (CAP) addition. The reactivation of PS IIrequired weak irradiation and was suppressed by CAP. However,PS I measured as P700 was very stable. The level of PS I measuredas P700 was not significantly reduced by the irradiation for12 h even in the presence of CAP while the level of Cyt b559,component of PS II, was decreased markedly. The function ofPS I before and after supra-high irradiation with CAP was examinedby comparing sizes of P700 oxidation induced by a short flash,by a continuous light, and by determination of O2-and ferredoxin-reduction.No difference was observed in PS I actions before and afterthe irradiation treatment. These results indicate that the PSI complex is very tolerant of supra-high irradiation. However,the cells grown under supra-high irradiance contained much fewerPS I and PS II complexes than Cyt b6–f complexes. Theformer levels were reduced to a half to one fourth of thosebefore growth while the level of Cyt b6–f complex wasnot reduced so much. A possible mechanism for changes in thylakoidcomposition under supra-high irradiation was discussed. (Received February 16, 1991; Accepted June 12, 1991)  相似文献   

5.
We have studied the inactivation of the water-oxidizing complexby exogenous, ‘general’ reductants in various typesof PS II membrane. Extraction of the 33, 23 and 17 kDa proteinsfrom PS II membranes rendered the functional Mn susceptibleto rapid solubilization by reductants such as hydroquinone,benzidine and ascorbate, while water analogs, such as NH2OH,inactivated the complex regardless of the presence of PS IIextrinsic proteins. The extent of the inactivation was dependenton the hydrophobicity of the reductants examined. Diphenylcarbazide,an efficient electron donor to Z+ and D+, did not inactivatethe Mn complex. As reported earlier [Ghanotakis et al. (1984)Biochim. Biophys. Acta 767: 524], weak illumination deceleratedthe inactivation of the complex by the various reductants. Kineticanalyses of the flash-induced protection provided evidence aboutthe nature of the light state that was not susceptible to thereductants. This state was generated and decayed with half timesof approximately 0.5 and 9 s, respectively. However, such lightprotection was diminished under Cl-depleted conditions,at slightly alkaline pH, or when ascorbate was employed as areductant. Furthermore, we observed that the oxidation of N,N,N',N'-tetramethyl-p-phenylenediamine,which reacts with the Mn complex, was accomplished as a biphasicreaction. The amount of the fast phase, which was almost eliminatedafter the reconstitution of the 33 kDa protein and Ca2+, wasapproximately 7 electron equivalents per 200 Chl. From theseresults, it is likely that the bulky, ‘general’reductants reduce the functional Mn directly by solubilizingMn from the complex in the same way as do the water analogs.The effectiveness of these reductants in the photoactivationof the apo-water-oxidizing complex is also discussed. (Received September 13, 1989; Accepted March 12, 1990)  相似文献   

6.
Regulation of the assembly of the photosystem I (PS I) complexin response to the light regime in the photosynthetic systemof cyanophytes was studied in Synechocystis PCC 6714. The relationshipbetween the assembly of the PS I complex and synthesis of Chla was examined by model experiments in which synthesis of Chla was controlled by two inhibitors, gabaculine (GAB) and 2,2'-dipyridyl(DP). Both inhibitors caused a change to a lower ratio of PSI to PS II even under light that normally induces a high ratioof PS I to PS II. The change in stoichiometry induced by theseinhibitors was suppressed when protein synthesis was inhibitedby chloram-phenicol, similarly to the change in the stoichiometryinduced by light that excites mainly PS I (PS I light). Comparisonof the levels of PS I, PS II and Cyt b6-f complexes per cellindicated that a selective suppression of the assembly of thePS I complex was induced by the inhibitors: the stoichiometricrelationship among PS I, PS II and Cyt b6-f complexes was identicalto that induced by PS I light or white light of high intensity.GAB induced a decrease in size of the phycobilisome also, whileDP did not, similarly to PS I light. The results indicate thatthe ratio of PS I to PS II can be changed by the control ofsynthesis of Chl a. They also suggest that control of the synthesisor supply of Chl a probably exerted at site(s) in or after theprocess of the Mg-protoporphyrin branch, is involved in themechanism of regulation of the assembly of the PS I complexin cyanophytes. (Received September 7, 1989; Accepted November 20, 1989)  相似文献   

7.
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   

8.
Light-induced changes in stoichiometry among three thylakoidcomponents, PS I, PS II and Cyt b6-f complexes, were studiedwith the cyanophyte Synechocystis PCC 6714. Special attentionwas paid to two aspects of the stoichiometric change; first,a comparison of the patterns of regulation in response to differencesin light-intensity with those induced by differences in light-quality,and second, the relationship between regulation of the stoichiometryand the steady state of the electron transport system. Resultsfor the former indicated that (1) the abundance of PS I on aper cell basis was reduced under white light at the intensityas high as that for light-saturation of photosynthesis, butPS I per cell was increased under low light-intensity, (2) PSII and Cyt b6-f complexes remained fairly constant, and (3)changes in the abundance of PS I depended strictly on proteinsynthesis. The pattern was identical with that of chromaticregulation. For the second problem, the redox steady-statesof Cyt f and P700 under white light of various intensities weredetermined by flash-spectroscopy. Results indicated that (1)Cyt f and P700 in cells grown under low light-intensity [highratio of PS I to PS II (PS I/PS II)] were markedly oxidizedwhen the cells were exposed to high light-intensity, while theyremained in the reduced state under low light-intensity. (2)After a decrease in the abundance of PS I, most of P700 remainedin the reduced state even under high light-intensity, whilethe level of reduced Cyt f remained low. (3) Both Cyt f andP700 in cells of low PS I/PS II were fully reduced under lowlight-intensity, and Cyt f reduction following the flash wasrapid, which indicates that the turnover of PS I limits theoverall rate of electron flow. After an increase in the abundanceof PS I, the electron transport recovered from the biased state.(4) The redox steady-state of the Cyt b6-f complex correlatedwell with the regulation of PS I/PS II while the state of thePQ pool did not. Based on these results, a working model ofthe regulation of assembly of the PS I complex, in which theredox steady-state of the Cyt b6-f complex is closely relatedto the primary signal, is proposed. (Received August 2, 1990; Accepted December 10, 1990)  相似文献   

9.
Target analysis of the PS II reaction in spinach thylakoidsshowed that the respective molecular masses of the catalyticunits for oxygen evolution and the reaction center are about120 kDa and 250 kDa based on a kinetic separation of the tworeaction rates. The size of the oxygen-evolving enzyme agreedwith that determined for the PS II preparation from a thermophiliccyanobacterium by the same means [Nugent and Atkinson (1984)FEBS Lett. 170: 89]. Single hit-inactivation of oxygen evolutionand the PS II reaction center units indicates that each functionis driven by a structurally assembled unit. (Received August 6, 1984; Accepted December 17, 1984)  相似文献   

10.
Oxygen-evolving photosystem II (PS II) particles isolated fromthe thermophilic cyanobacterium Synechococcus elongatus consistedof about twenty polypeptides. Six polypeptides were identifiedby reaction with specific antisera as constituent subunit polypeptidesof oxygen-evolving PS II reaction center complexes. The mostabundant polypeptides were the and ß subunits ofallophycocyanin. Comparison with the polypeptide profile ofisolated phycobilisomes, as well as immunoblotting with an antiserumagainst the large linker polypeptide, showed that the largelinker polypeptide or some proteolytic fragments of it werepresent in the preparation. Thus, each PS II particle is, inessence, an oxygen-evolving PS II complex that is associatedwith the core substructure of the phycobilisome. Cross-linkingexperiments indicated that fragments of the large linker polypeptidesare closely associated with one another and that the Chl-carrying47- kDa polypeptide is located in close proximity to the D2protein and the extrinsic 33-kDa protein. (Received November 12, 1991; Accepted January 23, 1992)  相似文献   

11.
Dark-grown cells of the mutant C-2A' of Scenedesmus obliquus,which lack chlorophyll and photosynthetic activities, developa fully functional photosynthetic apparatus after transfer tolight (Bishop and Senger. 1972, Senger and Bishop 1972). Afteronset of illumination PS II-activity increases rapidly. Simultaneouslythe apoproteins of the two PS II chlorophyll -protein complexesCP-a11–1 and CP-a11–2 (48 and 44 kDa) are formedat high rates, as shown by fluorography after 35S-label duringdifferent periods of development. Polypeptides with apparentmolecular weights of 32.5 (probably the manganese-binding polypeptideof the oxygen-evolving system), 19.5, 18, 17and 16.5 kDa aresynthesized with kinetics comparable to those of the 48 and44 kDa polypeptides. Whereas the apoproteins of CP-a11–1and CP-11–2 are already present in etioplasts and areheavily formed immediately after onset of illumination, thepolypeptides related to the light-harvesting complex CP-a/bcannot be detected in dark-grown cells and show high rates ofbiosynthesis only after a delay of about 1 hour. An asynchronousfashion of formation is also reported for the correspondingchlorophyll-protein complexes of PS II. Our findings prove astep-wise assembly of PS II during chloroplast development inC-2A', starting with small PS II-units composed of the core-complexes,which increase their amount of light-harvesting complexes duringfurther illumination. High values for PS II-activity/chlorophylland for the half-rise time of fluorescence-induction in earlystages of greening, which decrease rapidly during prolongedillumination, also indicate the change from a small to a largePS Il-unit. Furthermore, investigation of the formation of thylakoidmembrane polypeptides under the influence of different protein-biosynthesisinhibitors of 70 S- or 80 S-ribosomes by means of 35S-labeland subsequent fluorography revealed that most of these polypeptidesare coded by nuclear genes. Only bands at 68, 65.5, 53, 52,48, 44, 32.5, 16.5, 15 and 14.5 kDa were labelled in the presenceof 80 S-inhibitors indicating their chloroplast origin. 1Present address: Fachbereich Biologie-Botanik, Philipps-Universit?t,I.ahnberge, 3550 Marburg, Federal Republic of Germany. (Received April 14, 1986; Accepted August 13, 1986)  相似文献   

12.
Based on the electron-transport properties on the reducing side of the reaction center, photosystem II (PS II) in green plants and algae occurs in two distinct forms. Centers with efficient electron-transport from QA to plastoquinone (QB-reducing) account for 75% of the total PS II in the thylakoid membrane. Centers that are photochemically competent but unable to transfer electrons from QA to QB (QB-nonreducing) account for the remaining 25% of total PS II and do not participate in plastoquinone reduction. In Dunaliella salina, the pool size of QB-nonreducing centers changes transiently when the light regime is perturbed during cell growth. In cells grown under moderate illumination intensity (500 E m-2s-1), dark incubation induces an increase (half-time 45 min) in the QB-nonreducing pool size from 25% to 35% of the total PS II. Subsequent illumination of these cells restores the steady-state concentration of QB-nonreducing centers to 25%. In cells grown under low illumination intensity (30 µE m–2s–1), dark incubation elicits no change in the relative concentration of QB-nonreducing centers. However, a transfer of low-light grown cells to moderate light induces a rapid (half-time 10 min) decrease in the QB-nonreducing pool size and a concomitant increase in the QB-reducing pool size. These and other results are explained in terms of a pool of QB-nonreducing centers existing in a steady-state relationship with QB-reducing centers and with a photochemically silent form of PS II in the thylakoid membrane of D. salina. It is proposed that QB-nonreducing centers are an intermediate stage in the process of damage and repair of PS II. It is further proposed that cells regulate the inflow and outflow of centers from the QB-nonreducing pool to maintain a constant pool size of QB-nonreducing centers in the thylakoid membrane.Abbreviations Chl chlorophyll - PS photosystem - QA primary quinone electron acceptor of PS II - QB secondary quinone electron acceptor of PS II - LHC light harvesting complex - Fo non-variable fluorescence yield - Fpl intermediate fluorescence yield plateau level - Fmax maximum fluorescence yield - Fi mitial fluorescence yield increase from Fo to Fpl(Fpl-Fo) - Fv total variable fluorescence yield (Fmax-Fo) - DCMU dichlorophenyl-dimethylurea  相似文献   

13.
The interactions of benzoquinones with the reduced forms ofthe bound plastoquinone acceptors, QA and QB, were studied withoxygen-evolving photosystem II (PS II) particles from the thermophiliccyanobacterium Synechococcus elongatus, which largely lack poolplastoquinone molecules [Takahashi and Katoh (1986) Biochim.Biophys. Acta 845: 183]. Oxygen evolution in the presence ofvarious electron acceptors was determined and flash-inducedchanges in absorbance in the blue region were analyzed in termsof difference spectra, dependence on the concentration of benzoquinoneand on temperature, and sensitivity to 3-(3,4-dichlorophenyl)-1,1-dimethylurea(DCMU). The more hydrophobic the quinone molecule, the higherwas the rate of oxygen evolution, and the maximum rate of 3,000µmoles O2.(mg chlorophyll)–1.h–1 was recordedin the presence of phenyl- and dichloro-p-benzoquinones. DCMUinhibited oxygen evolution by more than 95%. However, spectrophotometricstudies revealed that, even though electrons were transferredto benzoquinones predominantly via the direct oxidation of by added benzoquinones occurred in such a way as to indicate thatabout 40% of PS II reaction centers were not associated withfunctional QB sites. was very stable in the presence of ferricyanide. However, benzoquinonesinduced the slow oxidation of . The characteristics of the benzoquinone reductioin in thePS II preparation is discussed. 1Present address: Department of Life Sciences, Faculty of Science,Himeji Institute of Technology, Shosha 2167, Himejishi, Hyogo-ken,671-22 Japan (Received May 8, 1990; Accepted August 14, 1990)  相似文献   

14.
Prenylquinones were extracted with hexane from lyophilized oxygen-evolvingphotosystem II particles prepared from spinach chloroplasts.Determination by high performance liquid chromatography showedthat two molecules of plastoquinone A remained per reactioncenter after the extraction, in contrast to the presence ofthree to four plastoquinone A molecules before the extraction.Electron transfer from water to phenyl-p-quinone was not inhibitedby the extraction. Measurement of EPR signal II and microsecondchlorophyll fluorescence kinetics showed that hexane did notextract quinones which were acting as the secondary electrondonor (Z) and the primary electron acceptor (QA) in photosystemII. These results, as well as the effect of quinone extractionon oxygen evolution, indicate that two molecules of plastoquinoneA acting as Z and QA are essential for the activity of photosystemII. An artificial donor phenyl-p-quinone probably accepts electronfrom QA at the same site as the intrinsic secondary electronacceptor (QB). QA and Z seem to be surrounded by special microenvironmentswhich differ from that of bulk quinones, and are resistant tohexane treatment. (Received November 27, 1984; Accepted April 30, 1985)  相似文献   

15.
Cytochrome b-559 in photosystem II can be characteristicallyconverted from a high- to a low-potential form. Taking thisresponse of Cyt b-559 as evidence for the denaturation of proteinmolecules, the sizes of the structures that stabilize the high-potentialform of Cyt b-559 in PS II membranes and thylakoids from spinachwere determined by radiation inactivation. When a target of26 kDa was inactivated in PS II membranes, Cyt b-559 was convertedto the low-potential form. The size was consistent with a molecularweight of Cyt b-559 in a proposed tetrameric structure thatconsists of two sets of 9.2-kDa and 4.3-kDa subunits [Widgeret al. (1985) FEBS Lett. 191: 186–190]. In contrast tothe functional size of 26 kDa in the PS II membranes, the functionalsize was 116 kDa in thylakoid membranes. The results suggestthe presence of an extra 90-kDa electron carrier between a redoxtitrator outside the membranes and the Cyt b-559, which maynot expose its active site to the surface of the thylakoids. (Received March 9, 1989; Accepted June 23, 1989)  相似文献   

16.
This study was done to confirm our previous observation withthe pattern of changes in electron transport composition inducedby an imbalance of the electron transport state. Contents ofphotosystem (PS) I and II complexes and their antennae and Cytb6/f complex were determined for systems of cyanobacterium SynechocystisPCC 6714 of different PS I/PS II ratios. The results indicatedthat (1) the observed changes in the PS I/PS II ratio are not-dueto regulation of the activities of the respective PS's but tochanges in their contents, (2) the molar ratio between PS IIand Cyt b6/f complexes was fairly constant when marked changesoccurred in the PS I content, and (3) the PS II and Cyt b6/fcontents per cell remained fairly constant while the PS I contentchanged markedly. These findings agree with our previous observationwith autotrophic cells of Anacystis nidulans Tx 20 and supportour argument that in cyanobacterial and red algal electron transportsystems, the content of the terminalcomponent(s), such as PSI complex, is regulated in order to maintain a balance betweenthe electron influx by PS II action to the system and the effluxby PS I action from it. (Received June 3, 1987; Accepted September 20, 1987)  相似文献   

17.
Cytochrome composition of the cyanobacterial photosyntheticsystem was studied with Anacystis nidulans (Tx 20) in relationto the chromatic regulation of photosystem composition. Comparisonof cytochrome compositions in cells with a high PS I/II ratio(3.0, grown under weak orange light) and with a low ratio (1.6,grown under weak red light) indicated that cytochrome compositionwas also changed in the chromatic regulation of photosystemcomposition. Two types of cytochrome change were observed: 1)contents of cytochromes C553 and c548 were changed in parallelwith the changes in PS I content, and 2) cytochrome b553 andcytochrome b6-f complex were held at a constant molar ratioto PS II. The molar ratio, PS II : cytochrome b559 : cytochromeb6-f complex : cytochrome c553 : PS I : cytochrome C548, inthe red-grown cells was 1 : 2.5 : 1.3 : 0.17 : 1.6 : 0.67, andthe ratio in the orange-grown cells, 1:2.4:0.9:0.32:3.0:1.2.In both types of cells, almost all cytochrome f in the cytochromeb6-f complex was rapidly oxidized after multiple flash activation,indicating that all cytochrome b6-f complexes in cells of bothtypes are functionally connected to PS I, even when the molarratio to PS I is largely changed. The content of cytochromeC553 was at most 0.14 of PS I, suggesting that the cytochrometurns over several times per one turnover of PS I. 1Present address: Department of Biology, Faculty of Science,Tokyo Metropolitan University, Fukazawa 2-1-1, Setagaya, Tokyo158, Japan. (Received January 20, 1986; Accepted March 17, 1986)  相似文献   

18.
Dark-grown cotyledons of pine (Pinus thunbergit) did not exhibitO2 evolution, but this capability was rapidly activated by illuminationfor a short period (photoactivation). To examine the biochemicalchanges which accompany the process of photoactivation in gymnosperms,a method enabling the preparation of highly active O2-evolvingphotosystem II (PS II) membranes was applied to light-grown,dark-grown, and photoactivated cotyledons. PS II membranes preparedfrom light-grown cotyledons exhibited high O2-evolving activity,and contained all the intrinsic proteins as well as the threeextrinsic proteins (32, 23 and 17 kDa) associated with PS II.These membranes were also found to contain 4.4 Mn and 0.83 Ca/PSII reaction center. PS II membranes from dark-grown cotyledonscontained all the intrinsic proteins, but preserved only 32kDa extrinsic protein, and zero Mn and 0.85 Ca/PS II reactioncenter. The two extrinsic proteins (23 and 17 kDa) absent inthe PS II membranes from dark-grown cotyledons were, however,present as mature forms in whole thylakoid membranes from thecorresponding sample. The PS II membranes isolated from photoactivatedcotyledons showed a high activity of O2 evolution and retainedthe three extrinsic proteins, 5.3 Mn and 1.1 Ca/PS II reactioncenter, respectively. The results indicated that Mn and thetwo extrinsic proteins were tightly integrated in the O2-evolvingapparatusduring the process of photoactivation but integration of Capreceded the integration of Mn by photoactivation. (Received December 9, 1991; Accepted February 1, 1992)  相似文献   

19.
The formation of Chl-protein complexes (CPs) in cucumber cotyledonsduring a dark period after a brief illumination was studied.SDS-PAGE analysis showed that the P700-Chl a-protein complex(CP1) and Chl a-protein complex of the PS II core (CPa) increased,with a concomitant decrease in the light-harvesting Chl a/6-proteincomplex of PS II (LHCII), during 24-h dark incubation of cotyledonsafter 6h of continuous illumination. In agreement with theseresults, curve analysis revealed that spectral components characteristicof CP1 and CPa increased while those of Chi b decreased duringthe dark incubation. Since Chl is not synthesized in the dark,Chl must be released from LHCII and re-incorporated into CP1and CPa. The amounts of apoproteins of CP1 and 43 kDa protein(one of the apoproteins of CPa) increased during the dark incubation,and the increase could be inhibited by chloramphenicol (CAP).CP1 did not increase in the dark when tissues were incubatedwith CAP which inhibited the synthesis of apoproteins of CP1,indicating that CP formation by Chl redistribution needs newlysynthesized apoproteins. The decrease in LHCII apoproteins duringdark incubation was inhibited by CAP probably because Chl wasnot removed from LHCII by apoproteins of CP1 and CPa, whosesynthesis was blocked by the presence of CAP. When intermittently-illuminatedcotyledons containing a little LHCII were incubated with CaCl2in the dark, Chl b and LHCII apoproteins accumulated with thedisappearance of 43 kDa protein; Chl of 43 kDa protein may beutilized for LHCII formation. We concluded that Chl moleculesonce bound with their apoproteins are redistributed among theapoproteins. (Received October 17, 1990; Accepted December 6, 1990)  相似文献   

20.
《FEBS letters》1987,217(1):53-56
The technique of (γ-ray) radiation inactivation has been used to estimate the functional sizes of the PS II centers (PS IIα and PS IIβ) responsible for the biphasicity of the fluorescence induction curve from DCMU-inhibited spinach chloroplasts. It is found that the size of PS IIα (266 ± 5 kDa) is almost twice as large as that of PS IIβ (135 ± 5 kDa). The result clearly indicates that the two types of PS II are structurally distinct and furthermore, the difference exists in the reaction center per se. Implications on the organization of PS II reaction centers are discussed.  相似文献   

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