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  • 1
    Electronic Resource
    Electronic Resource
    Regulation of Rubisco by inhibitors in the light (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Plant, cell & environment 20 (1997), S. 0 
    Details
    ISSN: 1365-3040
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: 2-carboxy-D-arabinitol-1-phosphate (CA1P) bound to Rubisco either in leaf extracts or after purification can be displaced by SO42− ions. Thus, treatment of leaf extracts with a buffer containing 200 mol m−3 SO42− displaces any bound CA1P and enables measurement of maximum car-boxylation potential. In tobacco leaves, the activity following treatment with SO4−2 ions (‘maximal activity’) is greater than the total Rubisco activity. The ratio of the two activities altered in a dynamic way with fluctuations in irradiance. Even in species which do not produce significant amounts of CA1P, the maximal activity greatly exceeded the total activity. Anion exchange separation of components in acid extracts confirmed the absence of CA1P in tobacco leaves harvested above an irradiance of 300 μmol quanta m−2 s−1, but the presence of another inhibitor of Rubisco. These results are consistent with the regulation of Rubisco activity by inhibitors other than CA1P which, like CA1P, can be displaced by SO42− ions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-3040.1997.d01-85.x
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  • 2
    Electronic Resource
    Electronic Resource
    A point mutation in the N-terminus of ribulose-1,5-bisphosphate carboxylase affects ribulose-1,5-bisphosphate binding (1991)
    Springer
    Planta 184 (1991), S. 35-39 
    Details
    ISSN: 1432-2048
    Keywords: Ribulose ; 1,5-bisphosphate carboxylase ; Gene mutation (N-terminus) ; Substrate affinity (ribulose-1,5-bisphosphate)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Mutagenesis in vitro of the gene encoding the large subunit of ribulose-1,5-bisphosphate carboxylase/ oxygenase (EC 4.1.1.39) from Anacystis nidulans was used to generate novel enzymes. Two conserved residues, threonine 4 and lysine 11 in the N-terminus were changed. The substitution of threonine 4 with serine or valine had little effect on the kinetic parameters. The substitution of lysine 11 with leucine, which is non-polar, increased the K m for ribulose-1,5-bisphosphate from 82 to 190 μM but its replacement with glutamine, which has polar properties, had no appreciable effect.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00208233
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  • 3
    Electronic Resource
    Electronic Resource
    A nocturnal inhibitor of carboxylation in leaves (1986)
    [s.l.] : Nature Publishing Group
    Nature 324 (1986), S. 274-276 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The method used to isolate the inhibitor from dark-treated plant material exploited its affinity for the active enzyme. The carboxylase was extracted and purified in buffer containing CO2 (HCO^) and Mg2+ so that the inhibitor remained bound. The specific carboxylase activity of the enzyme at the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/324274a0
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  • 4
    Electronic Resource
    Electronic Resource
    Daucic Acid and its Occurrence in Plants (1971)
    [s.l.] : Nature Publishing Group
    Nature 232 (1971), S. 423-424 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Bulk quantities of this acid, conveniently named daucic acid, were isolated from carrots (preferably mature) by extraction of the pulped roots with hot water. After the removal of solid material, the acid, together with nucleotide and polysaccharide material, was adsorbed on activated charcoal at ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/232423b0
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  • 5
    Electronic Resource
    Electronic Resource
    Photorespiratory nitrogen cycle (1978)
    [s.l.] : Nature Publishing Group
    Nature 275 (1978), S. 741-743 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] 2 GLYCINE + H2O SERINE + CO2 + NH3 + 2H+ + 2e- Photorespiration is considered wasteful because it loses CO2 and energy, but little emphasis has been placed on the simultaneous and stoichiometric release of NH3. Based on estimates of photorespiration in wheat leaves of 80 mol CO2 h-1 g-1 fresh ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/275741a0
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  • 6
    Electronic Resource
    Electronic Resource
    Mutations in loop six of the large subunit of ribulose-1,5-bisphosphate carboxylase affect substrate specificity (1992)
    Springer
    Planta 187 (1992), S. 109-112 
    Details
    ISSN: 1432-2048
    Keywords: Ribulose-1,5-bisphosphate carboxylase ; Gene mutation ; Specificity factor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Mutagenesis in vitro of the gene encoding the large subunit of ribulose-1,5-bisphosphate carboxylase/ oxygenase (EC 4.1.1.39) from Anacystis nidulans Synechococcus PCC 6301) was used to generate novel enzymes in Escherichia coli. Residues in C-terminal loop 6 of the β/α barrel structure of the large subunit were changed. Replacement of valine 331 with alanine caused a 90% reduction in V max but did not alter the enzyme's relative specificity towards either of its gaseous substrates, CO2 and O2. However replacement of alanine 340 with glutamate decreased the enzyme's specificity for CO2 but had no significant effect on either the K m for ribulose-1,5-bisphosphate or CO2 or on V max. In contrast replacing a small cassette of residues 338-341 produced a small increase in the specificity factor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00201631
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  • 7
    Electronic Resource
    Electronic Resource
    The state of activation of ribulose-1,5-bisphosphate carboxylase in wheat leaves (1987)
    Springer
    Photosynthesis research 11 (1987), S. 97-108 
    Details
    ISSN: 1573-5079
    Keywords: RuBP carboxylase ; wheat leaves ; photosynthesis ; activation ; orthophosphate ; carbon dioxide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In light and in darkness, exposure of leaf segments to CO2-free atmospheres caused a marked reduction in extractable RuBP carboxylase activity. By contrast, darkness caused a relatively small decrease in carboxylase activity in extracts from leaf segments kept in air containing CO2. Recovery of carboxylase activity in leaves during illumination in air after exposure to CO2-free conditions paralleled recovery of capacity for photosynthesis; in darkness recovery of carboxylase activity in leaves was slower than in the light. Extracts from leaves exposed to CO2-free conditions recovered activity when provided with CO2 and Mg2+; there were clearly, however, substances in the extracts that modified the activity achieved and caused anomalous decreases and increases with time after extraction. Studies of the effect of orthophosphate on the activity of purified wheat carboxylase in vitro were consistent with the view that many of the effects observed on the activity of crude leaf extracts were due to orthophosphate content.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00018268
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  • 8
    Electronic Resource
    Electronic Resource
    Purified Ribulose-P2 carboxylase from wheat with high specific activity and with fast activation (1984)
    Springer
    Photosynthesis research 5 (1984), S. 47-62 
    Details
    ISSN: 1573-5079
    Keywords: ribulose-P2 ; carboxylase ; wheat ; high specific activity ; fast activation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00018374
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  • 9
    Electronic Resource
    Electronic Resource
    Regulation of RuBP carboxylase activity associated with photo-inhibition of wheat (1982)
    Springer
    Photosynthesis research 3 (1982), S. 105-111 
    Details
    ISSN: 1573-5079
    Keywords: photo-inhibition ; RuBP carboxylase inactivation ; wheat leaves
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Detached wheat leaves were illuminated in air until a steady rate of photosynthesis was established. Then the gas was changed to 1% O2, 99% N2 and after 2.5 h further illumination the capacity of the leaves for photosynthesis in air was decreased to approximately 50%. Measurement of RuBP carboxylase activity in extracts showed that inhibition of photosynthesis was accompanied by 70% inactivation of this enzyme. The capacity for photosynthesis and the activity of RuBP carboxylase were recovered when leaves were returned to normal air. Extracts of the leaves made when photosynthesis and carboxylase activity were low, recovered most of the lost carboxylase activity when supplemented with bicarbonate and magnesium ions. The time courses for activation and inactivation of the RuBP carboxylase in these experiments suggests the operation of a mechanism that has not yet been elucidated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00040708
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