共查询到20条相似文献,搜索用时 15 毫秒
1.
L Rosa 《Biochemical and biophysical research communications》1979,88(1):154-162
Addition of ribose-5-phosphate to intact spinach chloroplasts in the absence of added Pi resulted in a conversion of part of the Benson-Calvin cycle into a linear sequence so that triose phosphate accumulated during CO2 fixation stoichiometrically with the O2 evolved (triose phosphate / O2 ratio was 2.0). The fortunate consequence of this effect is that the ratio may be calculated from the 3-phosphoglycerate and triose phosphate accumulated and the O2 evolved. In this way the ratio was shown to be 2.0, with cyclic or pseudocyclic phosphorylation contributing less than 9% to the total phosphorylation. 相似文献
2.
Photosynthetic electron transport capacity was varied in vivo in sugar beets using iron deficiency, and its effects on the light modulation of ribulose bisphosphate carboxylase (RuBPCase) studied. Three treatment groups corresponding to decreasing amounts of thylakoids per leaf area were examined: iron sufficient (control), moderately iron-stressed, and severely iron-stressed. Reduction in electron transport capacity in vivo was correlated with a substantial decrease in the level of RuBPCase activation, even at saturating irradiances. These results indicate a direct relationship between RuBPCase activation and photosynthetic electron transport. In addition, our data suggest that the activation of RuBPCase could not solely account for the increases in the photosynthetic rate at high irradiances; RuBPCase reached maximal activation at irradiances well below light saturation for net photosynthesis.Abbreviations Chl
chlorophyll
- FeCN
ferricyanide
- FBPase
fructose 1,6-bisphosphatase
- RuBP
ribulose 1,5-bisphosphate
- RuBPCase
ribulose 1,5-bisphosphate carboxylase
- SBPase
sedoheptulose 1,7-bisphosphatase 相似文献
3.
Abstract. A mechanistic model of photosynthesis is developed based on the characteristics of ribulose 1,5-bisphosphate (RuBP) carboxylase and the assimilation of CO2 as an ordered reaction with RuBP binding before CO2 . An equation is derived which considers the effects of light (for regeneration of RuBP) and CO2 . Taking values for the maximum turnover of RuBP carboxylase at substrate saturation, the maximum carboxylation efficiency (maximum increase in rate per increase in CO2 concentration) and the minimum quantum requirement for the C3 pathway, photosynthesis in the absence of photorespiration is simulated. In the model, at varying concentrations of CO2 , the efficiency of light utilization approaches a maximum value as photon flux density decreases. Similarly, with a given maximum carboxyation capacity, at varying photon flux densities the carboxylation efficiency approaches a constant maximum value (equal to V max / K m CO2 ) as CO2 is decreased. However, a decrease in the state of activation of RuBP carboxylase under low light results in a lower carboxylation efficiency. Limits on the rate of photosynthesis, as the maximum capacity for regeneration of RuBP is reduced relative to carboxylation potential, or as the maximum capacity of the carboxylase varies, are considered. 相似文献
4.
Stefan TimmAlexandra Florian Stephanie ArrivaultMark Stitt Alisdair R. FernieHermann Bauwe 《FEBS letters》2012,586(20):3692-3697
Photorespiration makes oxygenic photosynthesis possible by scavenging 2-phosphoglycolate. Hence, compromising photorespiration impairs photosynthesis. We examined whether facilitating photorespiratory carbon flow in turn accelerates photosynthesis and found that overexpression of the H-protein of glycine decarboxylase indeed considerably enhanced net-photosynthesis and growth of Arabidopsis thaliana. At the molecular level, lower glycine levels confirmed elevated GDC activity in vivo, and lower levels of the CO2 acceptor ribulose 1,5-bisphosphate indicated higher drain from CO2 fixation. Thus, the photorespiratory enzyme glycine decarboxylase appears as an important feed-back signaller that contributes to the control of the Calvin-Benson cycle and hence carbon flow through both photosynthesis and photorespiration. 相似文献
5.
A rapid method to determine the CO2/O2 specificity factor of ribulose 1,5-bisphosphate carboxylase/oxygenase is presented. The assay measures the amount of CO2 and O2 fixation at varying CO2/O2 ratios to determine the relative rates of each reaction. CO2 fixation is measured by the incorporation of the moles of14CO2 into 3-phosphoglycerate, while O2 fixation is determined by subtraction of the moles of CO2 fixed from the moles of RuBP consumed in each reaction. By analyzing the inorganic phosphate specifically hydrolyzed from RuBP under alkaline conditions, the amount of RuBP present before and after catalysis by rubisco can be determined. 相似文献
6.
Michael G. Klein Sarah C. Bagby Sallie W. Chisholm Sabine Heinhorst Cheryl A. Kerfeld 《Journal of molecular biology》2009,392(2):319-483
Bacterial microcompartments (BMCs) are polyhedral bodies, composed entirely of proteins, that function as organelles in bacteria; they promote subcellular processes by encapsulating and co-localizing targeted enzymes with their substrates. The best-characterized BMC is the carboxysome, a central part of the carbon-concentrating mechanism that greatly enhances carbon fixation in cyanobacteria and some chemoautotrophs. Here we report the first structural insights into the carboxysome of Prochlorococcus, the numerically dominant cyanobacterium in the world's oligotrophic oceans. Bioinformatic methods, substantiated by analysis of gene expression data, were used to identify a new carboxysome shell component, CsoS1D, in the genome of Prochlorococcus strain MED4; orthologs were subsequently found in all cyanobacteria. Two independent crystal structures of Prochlorococcus MED4 CsoS1D reveal three features not seen in any BMC-domain protein structure solved to date. First, CsoS1D is composed of a fused pair of BMC domains. Second, this double-domain protein trimerizes to form a novel pseudohexameric building block for incorporation into the carboxysome shell, and the trimers further dimerize, forming a two-tiered shell building block. Third, and most strikingly, the large pore formed at the 3-fold axis of symmetry appears to be gated. Each dimer of trimers contains one trimer with an open pore and one whose pore is obstructed due to side-chain conformations of two residues that are invariant among all CsoS1D orthologs. This is the first evidence of the potential for gated transport across the carboxysome shell and reveals a new type of building block for BMC shells. 相似文献
7.
《Bioscience, biotechnology, and biochemistry》2013,77(6):942-944
A non-radioisotopic anion-exchange ion chromatographic method for measuring the carboxylation/ oxygenation specificity (τ) of ribulose 1, 5-bisphosphate carboxylase/oxygenase (RubisCO) is presented. The assay measures the amounts of fixation products at varying [CO2]/[O2] ratios to measure the relative rates of CO2 and O2 fixation reactions. The amount of 3-phosphoglycerate (3-PGA) and phosphoglycolate (PG) in the reaction mixture were measured with a conductivity detector and the specific factor was calculated using the following equations: νc = ([3-PGA] – [PG])/2 and νo = [PG]. By this method, specificity factors for RubisCOs were measured without using radioactive reagents. 相似文献
8.
When envelope-free spinach chloroplasts are incubated with stromal protein, catalytic NADP, catalytic ADP, radioactive bicarbonate and fructose 1,6-bisphosphate, 14CO2 fixation starts immediately upon illumination but oxygen evolution is delayed. The delay is increased by the addition of fructose 6-phosphate and by a variety of factors known (or believed) to increase fructose bisphosphatase activity (such as dithiothreitol, more alkaline pH, higher [Mg] and antimycin A). Conversely, the lag can be decreased or eliminated by the addition of an ATP-generating system. Bearing in mind the known inhibition, by ADP, of sn-phospho-3-glycerate (3-phosphoglycerate) reduction it is concluded that the lag in O2 evolution results from the production of ribulose 5-phosphate from fructose bisphosphate and that this in turn inhibits the reoxidation of NADPH by adversely affecting the ADP/ATP ratio. The results are discussed in their relation to the mode of action of antimycin A and to regulation of the reductive pentose phosphate pathway. 相似文献
9.
10.
A.S. Bhagwat 《Phytochemistry》1982,21(2):285-289
Ribulose 1,5-bisphosphate carboxylase when activated by preincubation with 1 mM bicarbonate and 10 mM magnesium chloride can be further activated ca 20–500% by incubating with 2.5 mM phosphoglycolate depending upon the pH of the preincubation medium. The activation effects were seen only under specific preincubation conditions. The activation by phosphoglycolate was a slow reaction requiring ca 15 min for maximal effect. Even though magnesium was essential for phosphoglycolate activation, concentrations higher than 15 mM progressively inhibited the activation of the enzyme by phosphoglycolate. When added directly to the reaction mixture, phosphoglycolate was a potent inhibitor of the carboxylase activity. Even under preincubating conditions, phosphoglycolate showed slight inhibitory effect at 0.1 mM and activation was observed at concentrations higher than 0.5 mM. The KA value for phosphoglycolate was 2.8 mM. 相似文献
11.
12.
Christian Paech John Pierce Stephen D. McCurry N.E. Tolbert 《Biochemical and biophysical research communications》1978,83(3):1084-1092
Xylulose-1,5-bisphosphate in preparations of ribulose-1,5-bisphosphate (ribulose-P2) arises from non-enzymic epimerization and inhibits the enzyme. Another inhibitor, a diketo degradation product from ribulose-P2, is also present. Both compounds simulate the substrate inhibition of ribulose-P2 carboxylase/oxygenase previously reported for ribulose-P2. Freshly prepared ribulose-P2 had little inhibitory activity. The instability of ribulose-P2 may be one reason for a high level of ribulose-P2 carboxylase in chloroplasts where the molarity of active sites exceeds that of ribulose-P2. Because the KD of the enzyme/substrate complex is ≤1 μM, all ribulose-P2 generated in situ may be stored as this complex to prevent decomposition. 相似文献
13.
RuBPCO kinetics and the mechanism of CO2 entry in C3 plants 总被引:1,自引:1,他引:1
Abstract. The CO2 partial pressure in the chloroplasts of intact photosynthetic C3 leaves is thought to be less than the intercellular CO2 partial pressure. The intercellular CO2 partial pressure can be calculated from CO2 and H2O gas exchange measurements, whereas the CO2 partial pressure in the chloroplasts is unknown. The conductance of CO2 from the intercellular space to the chloroplast stroma and the CO2 partial pressure in the chloroplast stroma can be calculated if the properties of photosynthetic gas exchange are compared with the kinetics of the enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBPCO). A discrepancy between gas exchange and RuBPCO kinetics can be attributed to a deviation of CO2 partial pressure in the chloroplast stroma from that calculated in the intercellular space. This paper is concerned with the following: estimation of the kinetic constants of RuBPCO and their comparison with the CO2 compensation concentration; their comparison with differential uptake of 14CO2 and 12CO2; and their comparison with O2 dependence of net CO2 uptake of photosynthetic leaves. Discrepancy between RuBPCO kinetics and gas exchange was found at a temperature of 12.5 °C, a photosynthetic photon flux density (PPFD) of 550 μmol quanta m?2 s?1, and an ambient CO2 partial pressure of 40 Pa. Consistency between RuBPCO kinetics and gas exchange was found if CO2 partial pressure was decreased, temperature incresed and PPFD decreased. The results suggest that a discrepancy between RuBPCO kinetics and gas exchange is due to a diffusion resistance for CO2 across the chloroplast envelope which decreases with increasing temperature. At low CO2 partial pressure, the diffusion resistance appears to be counterbalanced by active CO2 (or HCO3) transport with high affinity and low maximum velocity. At low PPFD, CO2 partial pressure in the chloroplast stroma appears to be in equilibrium with that in the intercellular space due to low CO2 flux. 相似文献
14.
Iancu CV Ding HJ Morris DM Dias DP Gonzales AD Martino A Jensen GJ 《Journal of molecular biology》2007,372(3):764-773
Carboxysomes are organelle-like polyhedral bodies found in cyanobacteria and many chemoautotrophic bacteria that are thought to facilitate carbon fixation. Carboxysomes are bounded by a proteinaceous outer shell and filled with ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO), the first enzyme in the CO(2) fixation pathway, but exactly how they enhance carbon fixation is unclear. Here we report the three-dimensional structure of purified carboxysomes from Synechococcus species strain WH8102 as revealed by electron cryotomography. We found that while the sizes of individual carboxysomes in this organism varied from 114 nm to 137 nm, surprisingly, all were approximately icosahedral. There were on average approximately 250 RuBisCOs per carboxysome, organized into three to four concentric layers. Some models of carboxysome function depend on specific contacts between individual RuBisCOs and the shell, but no evidence of such contacts was found: no systematic patterns of connecting densities or RuBisCO positions against the shell's presumed hexagonal lattice could be discerned, and simulations showed that packing forces alone could account for the layered organization of RuBisCOs. 相似文献
15.
16.
T Takabe A Incharoensakdi T Akazawa 《Biochemical and biophysical research communications》1984,122(2):763-769
The small subunit (B) of ribulose 1,5-bisphosphate (RuBP) carboxylase/oxygenase from Aphanothece halophytica is absolutely required for the catalysis, but depletion of subunit B does not significantly affect the formation of the quaternary complex-[enzyme.activator CO2.Mg.carboxyarabinitol bisphosphate] in the catalytic core. The inhibition of RuBP carboxylase activity by the reaction of the epsilon-amino group of a lysine in the RuBP-binding site with pyridoxal 5-P is the same whether subunit B is added to the catalytic core before or after the inactivating reaction. The function of subunit B is not related to the substrate binding. 相似文献
17.
Wei Dai Muyuan Chen Christopher Myers Steven J. Ludtke B. Montgomery Pettitt Jonathan A. King Michael F. Schmid Wah Chiu 《Journal of molecular biology》2018,430(21):4156-4167
Cyanobacteria are photosynthetic organisms responsible for ~ 25% of the organic carbon fixation on earth. A key step in carbon fixation is catalyzed by ribulose bisphosphate carboxylase/oxygenase (RuBisCO), the most abundant enzyme in the biosphere. Applying Zernike phase-contrast electron cryo-tomography and automated annotation, we identified individual RuBisCO molecules and their assembly intermediates leading to the formation of carboxysomes inside Syn5 cyanophage infected cyanobacteria Synechococcus sp. WH8109 cells. Surprisingly, more RuBisCO molecules were found to be present as cytosolic free-standing complexes or clusters than as packaged assemblies inside carboxysomes. Cytosolic RuBisCO clusters and partially assembled carboxysomes identified in the cell tomograms support a concurrent assembly model involving both the protein shell and the enclosed RuBisCO. In mature carboxysomes, RuBisCO is neither randomly nor strictly icosahedrally packed within protein shells of variable sizes. A time-averaged molecular dynamics simulation showed a semi-liquid probability distribution of the RuBisCO in carboxysomes and correlated well with carboxysome subtomogram averages. Our structural observations reveal the various stages of RuBisCO assemblies, which could be important for understanding cellular function. 相似文献
18.
Activation of Rubisco controls CO<Subscript>2</Subscript> assimilation in light: a perspective on its discovery 总被引:2,自引:0,他引:2
Jensen R 《Photosynthesis research》2004,82(2):187-193
CO2 fixation during photosynthesis is regulated by the activity of ribulose bisphosphate carboxylase (Rubisco). This conclusion
became more apparent to me after CO2-fixation experiments using isolated spinach chloroplasts and protoplasts, purified Rubisco enzyme, and intact leaves. Ribulose
bisphosphate (RuBP) pools and activation of Rubisco were measured and compared to 14CO2 fixation in light. The rates of 14CO 2 assimilation best followed the changes in Rubisco activation under moderate to high light intensities. RuBP pool sizes regulated
14
2 assimilation only in very high CO2 levels, low light and in darkness. Activation of Rubisco involves two separate processes: carbamylation of the protein and
removal of inhibitors blocking carbamylation or blocking RuBP binding to carbamylated sites before reaction with CO2 or O2.
This revised version was published online in June 2006 with corrections to the Cover Date. 相似文献
19.
Crafts-Brandner Steven J. Salvucci Michael E. Egli Dennis B. 《Photosynthesis research》1990,23(2):223-230
The abundances of ribulose-1,5-bisphosphate carboxylate/oxygenase (Rubisco) and ribulose-5-phosphate (Ru5P) kinase in field-grown soybean (Glycine max L. Merr.) leaves were quantified by a Western blot technique and related to changes in chlorophyll and photosynthetic capacity during senescence. Even though the leaf content of Rubisco was approximately 80-fold greater than that of Ru5P kinase, the decline in the levels of these two Calvin cycle enzymes occurred in parallel during the senescence of the leaves. Moreover, the decrease in the content of Rubisco was accompanied by parallel decreases of both the large and small subunits of this enzyme but not by an accumulation of altered large or small subunit isoforms. With increasing senescence, decreases in abundances of Rubisco, Ru5P kinase and chlorophyll were closely correlated with the decline in photosynthetic capacity; thus, the specific photosynthetic capacity when expressed per abundance of any of these parameters was rather constant despite an 8-fold decrease in photosynthetic capacity. These results suggest that during senescence of soybean leaves the chloroplast is subject to autolysis by mechanisms causing an approximately 80-fold greater rate of loss of Rubisco than Ru5P kinase.Jointly supported by the United States Department of Agricultural Research Service and the Kentucky Agricultural Experiment Station, Lexington (paper No. 88 3 286).Mention of a commercial product does not constitute endorsement by the United States Department of Agriculture. 相似文献
20.
Ribulose 1,5-bisphosphate carboxylase/oxygenase has been reported to occur in multiple forms in mung bean (Phaseolus aureus) using Sephadex G-200 chromatography. We have isolated this enzyme by identical methodology. The profile from Sephadex G-200 chromatography shows only one peak in contrast to the previous report and we find no evidence to corroborate the conclusions. Where Vc, Vo and Kc, Ko represent Vmax and Michaelis constants, respectively, the constant VcKo/VoKc for the single form is 70 at 40 μM CO2 and 1200 μM O2. 相似文献