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Monday, October 12, 2020 | History

2 edition of Ribulose bisphosphate carboxylase-oxygenase found in the catalog.

Ribulose bisphosphate carboxylase-oxygenase

Ribulose bisphosphate carboxylase-oxygenase

proceedings of a Royal Society discussion meeting held on 4 and 5 December 1985

  • 88 Want to read
  • 13 Currently reading

Published by The Royal Society of London in London .
Written in English

    Subjects:
  • Photosynthesis,
  • Ribulose-1, 5-bisphosphate carboxylase/oxygenase.,
  • Plants -- Photorespiration.

  • Edition Notes

    Statementorganized and edited by R. J. Ellis and J. C. Gray.
    ContributionsEllis, R. J. 1935-, Gray, J. C., Royal Society (Great Britain)
    Classifications
    LC ClassificationsQK898E58 R53 1986
    The Physical Object
    Paginationp. 305-469 (165 p.), [2] leaves of plates :
    Number of Pages469
    ID Numbers
    Open LibraryOL16682915M
    ISBN 100854032851

      Abstract. We have characterized the gene encoding ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) of the hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1. The gene encoded a protein consisting of amino acid residues, corresponding in size to the large subunit of previously reported Rubiscos. Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the primary carboxylating enzyme used by all photosynthetic organisms to incorporate atmospheric CO 2 into carbohydrate needed for growth and development. Nearly all of the carbon atoms that are present in living organisms have passed through the active site of Size: 2MB.

    Inside plant cells, the enzyme ribulose bisphosphate carboxylase/oxygenase (rubisco, shown here from PDB entry 1rcx) forms the bridge between life and the lifeless, creating organic carbon from the inorganic carbon dioxide in the air. Rubisco takes carbon dioxide and attaches it to ribulose bisphosphate, a short sugar chain with five carbon atoms. The effect of ozone (O 3) on the carboxylation activity of ribulose‐1,5‐bisphosphate carboxylase/oxygenase (Rubisco) from the fifth youngest leaf of four cultivars of Solarium tuberosum L. (potato) was investigated. Ozone‐tolerant cultivars ‘Superior’ (SP) and ‘Norgold Russet’ (NR), and O 3 ‐sensitive cultivars ‘Cherokee’ (CK) and ‘Norland’ (NL) were exposed to Cited by:

    RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process (PubMed). Both reactions occur simultaneously and in competition at the same active site. Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) enzymes from different species differ with respect to carboxylation catalytic efficiency and CO2/O2 specificity, but .


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Ribulose bisphosphate carboxylase-oxygenase Download PDF EPUB FB2

Richard C. Leegood, Robert P. Walker, in C4 Plant Biology, A Ribulose-l,5-bisphosphate Carboxylase–Oxygenase. All the C 4 acid decarboxylases release CO 2 for fixation by ribulose-1,5-bisphosphate carboxylase-oxygenase (Rubisco) in the bundle sheath.

The absence of carbonic anhydrase in bundle-sheath cells is of critical importance in ensuring that this CO 2. Katia Wostrikoff, David B. Stern, in The Chlamydomonas Sourcebook, I. Introduction. Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco; EC ) catalyzes the addition of gaseous carbon dioxide to ribulose-1,5-bisphosphate (RuBP), generating two molecules of 3-phosphoglyceric acid (3-PGA), and is thus the key enzyme in CO 2.

The enzyme ribulose bisphosphate carboxylase/oxygenase, or rubisco, fixes carbon dioxide. The carbon dioxide is incorporated into a five-carbon compound, which is. RIBULOSE 1, 5-BISPHOSPHATE CARBOXYLASE-OXYGENASE [Jensen, Richard G & Bahr, James T] on *FREE* shipping on qualifying offers.

RIBULOSE 1, 5-BISPHOSPHATE CARBOXYLASE-OXYGENASEAuthor: James T Jensen, Richard G & Bahr. Describe the oxygenase activity of ribulose 1,5-bisphosphate carboxylase/oxygenase (rubisco) and explain why this reaction is undesirable from the point of view of a plant.

The condensation of molecular oxygen with ribulose 1,5-bisphosphate yields 3-phosphoglycerate and the two-carbon compound phosphoglycolate.

Abstract. In some plants, 2-carboxy-d-arabinitol 1-phosphate (CA 1P) is tightly bound to catalytic sites of ribulose, 1,5-bisphosphate carboxylase/oxygenase (rubisco).This inhibitor's tight binding property results from its close resemblance to the Ribulose bisphosphate carboxylase-oxygenase book state intermediate of Cited by:   The RbcS gene for the small subunit of the chloroplast photosynthetic enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is a much studied example of a gene that has so migrated.

In green algae and higher plants, Rbc S has been transferred from the ancestral plastid's genome to become a nuclear multigene family (Rodermel, ).Cited by: Ribulose-1,5-Bis-Phosphate Carboxylase/Oxygenase Accumulation Factor1 is required for holoenzyme assembly in maize.

Plant Cell – [PMC free article] Goloubinoff P., Gatenby A.A., Lorimer G.H. GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia by: 1.

The enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyzes the formation of organic molecules from CO 2.

As the major enzyme of all photosynthetic cells, Rubisco is the most abundant protein on Earth. There is, however, a major catalytic flaw in the ability of this enzyme to convert CO 2 to Read More.

The element of-amino group of Lys of Rhodospirillum rubrum ribulosebisphosphate carboxylase/oxygenase was postulated as the essential base which initiates catalysis by abstracting the proton at C-3 or ribulose 1,5-bisphosphate.

ribulose 1,5-bisphosphate carboxylase/oxygenase [¦rībyə‚lo ¦wən ¦fiv ‚bis¦fäs‚fāt kä¦bäksə‚lās ′äksəjə‚nās]. Net photosynthesis, ribulose 1,5-bisphosphate (RuBP) and ATP contents, and ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBPCO) activities were followed before and after changing to 20 kPa p(O 2).

At 20°C, lowering p(O 2) increased net photosynthesis by 37%. This increase corresponded closely with the increase expected from the effect on Cited by:   The regulation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activity by 2-carboxyarabinitol 1-phosphate (CA1P) was investigated using gas-exchange analysis of antisense tobacco (Nicotiana tabacum) plants containing reduced levels of Rubisco activase.

When an increase in light flux from darkness to μmol quanta m−2 s−1 was followed, the Cited by:   The pyrenoid is a proteinaceous structure found in the chloroplast of most unicellular algae.

Various studies indicate that ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is present in the pyrenoid, although the fraction of Rubisco localized there remains controversial.

Estimates of the amount of Rubisco in the pyrenoid of Cited by: Inhibition of ribulose-1,5-bisphosphate carboxylase/oxygenase by ribulose-1,5-bisphosphate epimerization and degradation products. Biochemical and Biophysical Research Communications83 (3), Cited by:   Transgenic tobacco (Nicotiana tabacum L.

W38) with an antisense gene directed against the mRNA of the ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) small subunit was used to determine the kinetic properties of Rubisco in vivo. The leaves of these plants contained only 34% as much Rubisco as those of the wild type, but other photosynthetic Cited by: Ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) from spinach is a hexadecamer (L8S8, Mr = ,) consisting of eight large (L, residues) and eight small subunits (S, residues).

High-resolution data collection on crystals with larg Cited by:   Cloning and expression of the d-ribulose-1,5-bisphosphate carboxylase/oxygenase form II gene from Thiobacillus intermedius in Escherichia coli Ribulose bisphosphate carboxylase of the procaryotic symbiont of a hydrothermal vent tube worm: kinetics, activity and gene hybridizationCited by:   d-Ribulose-1,5-bisphosphate carboxylase/oxygenase has been purified fold from malate-grown Thiocapsa roseopersicina by salting out the enzyme from the high-speed supernatant between 68–95% saturation with respect to (NH4)2SO4, gelfiltration through Sephadex G, and DEAE-cellulose chromatography followed by sedimentation into a Cited by: 9.

Rubisco | High Quality Content by WIKIPEDIA articles Ribulose-1,5-bisphosphate carboxylase oxygenase, commonly known by the shorter name RuBisCO, is an enzyme involved in the first major step of carbon fixation, a process by which atmospheric carbon dioxide is converted by plants to energy-rich molecules such as glucose.

Ribulose-1,5-bisphosphate carboxylase oxygenase, better known as RuBisCO, is an enzyme that catalyzes the first major step of carbon fixation in the Calvin fixation is a process by which the atoms of atmospheric carbon dioxide are made available to organisms in the form of energy-rich molecules such as O splits 6-C molecules into two equal parts.

(biochemistry) An enzyme involved in the first major step of carbon fixation.Add tags for "Ribulose bisphosphate carboxylase-oxygenase: proceedings of a Royal Society discussion meeting held on 4 and 5 December ". Be the first. Similar Items.