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Relevant bibliographies by topics / Ribulose 1-5-bisphosphate carboxylase

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Academic literature on the topic 'Ribulose 1-5-bisphosphate carboxylase'

Author: Grafiati

Published: 4 June 2021

Last updated: 15 February 2022

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Journal articles on the topic "Ribulose 1-5-bisphosphate carboxylase"

1

Knaff, David B. "Structure and regulation of ribulose-1, 5-bisphosphate carboxylase/oxygenase." Trends in Biochemical Sciences 14, no. 5 (1989): 159–60. http://dx.doi.org/10.1016/0968-0004(89)90264-8.

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Yokota, Akiho, Atsushi Harada, and Shozaburo Kitaoka. "Characterization of Ribulose 1, 5-Bisphosphate Carboxylase/Oxygenase from Euglena gracilis Z1." Journal of Biochemistry 105, no. 3 (1989): 400–405. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a122676.

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BEESON, R. C. "Ribulose 1, 5-bisphosphate Carboxylase/ Oxygenase Activities in Leaves of Greenhouse Roses." Journal of Experimental Botany 41, no. 1 (1990): 59–65. http://dx.doi.org/10.1093/jxb/41.1.59.

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Varaljay, Vanessa A., Sriram Satagopan, Justin A. North, et al. "Functional metagenomic selection of ribulose 1, 5-bisphosphate carboxylase/oxygenase from uncultivated bacteria." Environmental Microbiology 18, no. 4 (2016): 1187–99. http://dx.doi.org/10.1111/1462-2920.13138.

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Maheshwari, Chirag, Robert A. Coe, Shanta Karki, et al. "Targeted knockdown of ribulose-1, 5-bisphosphate carboxylase-oxygenase in rice mesophyll cells." Journal of Plant Physiology 260 (May 2021): 153395. http://dx.doi.org/10.1016/j.jplph.2021.153395.

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Kane, HJ, J. Viil, B. Entsch, K. Paul, MK Morell, and TJ Andrews. "An Improved Method for Measuring the CO2/O2 Specificity of Ribulosebisphosphate Carboxylase-Oxygenase." Functional Plant Biology 21, no. 4 (1994): 449. http://dx.doi.org/10.1071/pp9940449.

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A simple, but very reproducible, method for measuring the relative specificity of ribulosebisphosphate carboxylase-oxygenase for CO2, as opposed to O2, is described. The method uses [1-14C]ribulose bisphosphate as substrate and combines the advantages of supplying both gaseous substrates from the gas phase with HPLC separation of the labelled products. Volumetric or gravimetric accuracy is not required at any stage of the procedure and variations in ionic strength and pH have little effect on the measurements. This leads to excellent reproducibility without the need for normalisation. The aver

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Gutteridge, S., G. S. Reddy, and G. Lorimer. "The synthesis and purification of 2′-carboxy-d-arabinitol 1-phosphate, a natural inhibitor of ribulose 1,5-bisphosphate carboxylase, investigated by31P n.m.r." Biochemical Journal 260, no. 3 (1989): 711–16. http://dx.doi.org/10.1042/bj2600711.

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2′-Carboxy-D-arabinitol 1-phosphate (2CA1P), a natural inhibitor of ribulose 1,5-bisphosphate carboxylase was synthesized from 2′-carboxy-D-arabinitol 1,5-bisphosphate (2CABP). The selective dephosphorylation of 2CABP with either acid phosphatase or alkaline phosphatase was investigated by using 31P n.m.r. The n.m.r. spectra of the progress of the reactions indicated that both phosphatases preferentially removed the 5-phosphate from the bisphosphate. After the consumption of all of the bisphosphate, alkaline phosphatase generated a mixture of 2′-carboxy-D-arabinitol 1- and 5-monophosphates in

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StiborovÁ, Marie. "Cd2+ Ions Affect the Quaternary Structure of Ribulose-1, 5-bisphosphate Carboxylase from Barley Leaves." Biochemie und Physiologie der Pflanzen 183, no. 5 (1988): 371–78. http://dx.doi.org/10.1016/s0015-3796(88)80045-3.

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ZHANG, Lie-Feng, Qi RUI, and Lang-Lai XU. "Degradation of the Large Subunit of Ribulose-1, 5-Bisphosphate Carboxylase/Oxygenase in Wheat Leaves." Journal of Integrative Plant Biology 47, no. 1 (2005): 60–66. http://dx.doi.org/10.1111/j.1744-7909.2005.00011.x.

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LI, Guofu. "Dithiothreitol decreases the thermal stability and unfolding coperativity of ribulose-1, 5-bisphosphate carboxylase/oxygenase." Progress in Natural Science 13, no. 3 (2003): 196. http://dx.doi.org/10.1360/03jz9035.

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Dissertations / Theses on the topic "Ribulose 1-5-bisphosphate carboxylase"

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Prescott, A. G. "The genetic manipulation of ribulose-1, 5-bisphosphate carboxylase/oxygenase." Thesis, University of East Anglia, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.380961.

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Bainbridge, Graeme. "Investigation into the structure and function relationships in Ribulose-1, 5-bisphosphate carboxylase/oxygenase." Thesis, Birkbeck (University of London), 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.309674.

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Maeda, Norihiro. "Studies on a novel type ribulose 1, 5-bisphosphate carboxylase/oxygenase from a hyperthermophilic archaeon, Thermococcus kodakaraensis KDO1." 京都大学 (Kyoto University), 2002. http://hdl.handle.net/2433/149817.

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Aono, Riku. "Studies on nucleotide and pentose metabolism in Archaea." 京都大学 (Kyoto University), 2015. http://hdl.handle.net/2433/200451.

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Amiel, Colette. "Contribution à l'étude de la scénescence foliaire chez le tournesol étude de la dégradation de la ribulose 1-5 bisphosphate carboxylase oxygénase /." Grenoble 2 : ANRT, 1988. http://catalogue.bnf.fr/ark:/12148/cb37611297k.

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Amiel, Colette. "Contribution a l'etude de la senescence foliaire chez le tournesol : etude de la degradation de la ribulose 1-5 bisphosphate carboxylase oxygenase." Toulouse 3, 1988. http://www.theses.fr/1988TOU30224.

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(. . . ) il a pu etre montre que la proteolyse foliaire est liee a l'apparition de l'inflorescence et, que l'azote libere migre pour une grande part vers le capitule. La ribulose 1-5 bisphosphate carboxylase oxygenase (rubisco) represente 50% des proteines solubles. L'etude de son hydrolyse a fait l'objet de la suite de ce travail. Pour definir les modalites et la localisation de la degradation, une methode d'obtention de protoplastes et de chloroplastes a aete mise au point. (. . . )

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Sasanuma, Tsuneo. "Molecular Evolutionary Analysis of the Multigene Family of the Small Subunit of Ribulose-1, 5-Bisphosphate Carboxylase/Oxygenase(rbcS)in Wheat and its Relatives." Kyoto University, 1999. http://hdl.handle.net/2433/181903.

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Kyoto University (京都大学)<br>0048<br>新制・課程博士<br>博士(農学)<br>甲第7894号<br>農博第1052号<br>新制||農||779(附属図書館)<br>学位論文||H11||N3257(農学部図書室)<br>UT51-99-G488<br>京都大学大学院農学研究科応用生物科学専攻<br>(主査)教授遠藤隆, 教授大西近江, 教授佐々木義之<br>学位規則第4条第1項該当

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Witte, Brian Hurin. "Taming the Wild RubisCO: Explorations in Functional Metagenomics." The Ohio State University, 2012. http://rave.ohiolink.edu/etdc/view?acc_num=osu1331562390.

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Sailland, Alain. "Etude de la structure primaire de la petite sous-unité de la ribulose-1, 5-bisphosphate carboxylase/oxygénase d'Euglena gracilis début de caractérisation du gène correspondant /." Grenoble 2 : ANRT, 1987. http://catalogue.bnf.fr/ark:/12148/cb37609614w.

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Zachová, Lucie. "Účinek zvýšené koncentrace oxidu uhličitého na množství a aktivitu enzymu Rubisco." Master's thesis, Vysoké učení technické v Brně. Fakulta chemická, 2008. http://www.nusl.cz/ntk/nusl-216364.

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In this diploma work changes of initial and total activities and content of Rubisco in beech and Norway spruce were studied. The plants were cultivated in conditions with ambient CO2 concentration (350 mol·mol–1) and elevated CO2 concentration (700 mol·mol–1). Three series of samples (at the beginning, in the middle and at the end of growing season) were taken. Initial and total Rubisco activities were measured spectrophotometrically and activation state was calculated. Rubisco content was determined by SDS–PAGE method. Rubisco activity in beech cultivated in elevated CO2 concentration decreas

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Books on the topic "Ribulose 1-5-bisphosphate carboxylase"

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1935-, Ellis R. J., Gray J. C, and Royal Society (Great Britain), eds. Ribulose bisphosphate carboxylase-oxygenase: Proceedings of a Royal Society discussion meeting held on 4 and 5 December 1985. The Royal Society of London, 1986.

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Book chapters on the topic "Ribulose 1-5-bisphosphate carboxylase"

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Knight, Stefan, Inger Andersson, Carl-Ivar Branden, and George Lorimer. "Structural Studies of Ribulose-1, 5-Bisphosphate Carboxylase/Oxygenase from Spinach." In Synchrotron Radiation in Structural Biology. Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-8041-2_14.

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Wang, Z. Y., S. Luo, K. Sato, M. Kobayashi, and T. Nozawa. "Measurements of Ribulose 1, 5-Bisphosphate Carboxylase/Oxygenase Activities by NMR." In Photosynthesis: Mechanisms and Effects. Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_786.

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Akazawa, T., A. Incharoensakdi, and T. Takabe. "Ribulose-1, 5-Bisphosphate Carboxylase/Oxygenase (Rubisco) (Isolation, Structure, and Regulation)." In Carbon Dioxide as a Source of Carbon. Springer Netherlands, 1987. http://dx.doi.org/10.1007/978-94-009-3923-3_6.

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Sachar, R. C., Daman Saluja, and P. Murali. "Structure, Function and Regulation of Ribulose 1, 5-Bisphosphate Carboxylase in Higher Plants." In Photosynthesis: Photoreactions to Plant Productivity. Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-2708-0_11.

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Osafune, Tetsuaki, Shuji Sumida, Akiho Yokota, and Eiji Hase. "Immunogold Localization of Ribulose-1, 5-Bisphosphate Carboxylase in Synchronized Cells of Euglena gracilis Z." In Current Research in Photosynthesis. Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0511-5_525.

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6

Brändén, Rolf, Kristina Janson, and Peter Nilsson. "Studies of the Co2+-Activated Ribulose-1, 5-Bisphosphate Carboxylase/Oxygenase by the Use of Spectrophotometry." In Techniques and New Developments in Photosynthesis Research. Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-8571-4_48.

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Gallagher, Thomas F. "Protein Binding Domains in the 5’-Upstream Region of Ribulose Bisphosphate Carboxylase Small Subunit Genes." In Plant Molecular Biology. Springer US, 1987. http://dx.doi.org/10.1007/978-1-4615-7598-6_73.

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8

Dalton, David R. "Working in the Dark." In The Chemistry of Wine. Oxford University Press, 2018. http://dx.doi.org/10.1093/oso/9780190687199.003.0019.

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Three turns of the Calvin cycle (Figure 11.1), allow the conversion of three (3) equivalents of carbon dioxide (CO2) (i.e., 3 C1 units) along with three (3) equivalents of the five-carbon carbohydrate derivative, ribulose-1,5-bisphosphate (i.e., 3 C5 units) to yield three (3) not yet isolated six-carbon adducts, 2-carboxy-3-ketoribitol-1,5-bisphosphate (3 C1 + 3 C5 = 3 C6) to form. The three (3) C6 species then undergo fragmentation to yield six (6) equivalents of the three (3) carbon dihydroxy monocarboxylate, 3-phosphoglycerate (i.e., 3 C6 = 6 C3). A cartoon representation of this process is shown in Scheme 11.1 for one of the three CO2 units. Of the six (6) three-carbon unit equivalents, five (5) are used to regenerate three (3) equiv¬alents of ribulose-1,5-bisphosphate (i.e., 5 C3 = 3 C5), while the sixth three- carbon fragment is now available to combine with another to make a six (6) carbon sugar (2 C3 = 1 C6) such as glucose (C6H12O6) (Figure 11.2). Additionally, as shown in Figure 11.3, 3-phosphoglycerate can be used to make other small compound building blocks such as glyceric acid, lactic acid, pyruvic acid and even acetic acid (after decarboxylation). Ribulose- 1,5-bisphosphate (often abbreviated as RuBP), using the enzyme ribulose- 1,5- bisphosphate carboxylase (EC 4.1.1.39, carboxydismutase, rubisco), catalyzes the Mg2+- dependent conversion of the 1,5- bisphosphate ester of the carbohydrate ribulose with carbon dioxide (CO2) to produce two (2) equivalents of 3- phosphoglycerate (PGA). As shown in the Schemes 11.1 and 11.2. A hypothetical the six carbon intermediate, 2- carboxy- 3- ketoribitol- 1,5- bisphosphate, is often written. It is important to keep in mind that we want the 3- phosphoglycerate for purposes of construction of other important compounds. But, as noted above, three turns of the cycle are necessary to produce six (6) equivalents of 3- phosphoglycerate, and five (5) of them are reused in making the three (3) ribulose- 1,5- bisphosphates necessary to turn the cycle three (3) times.

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Atomi, Haruyuki, Satoshi Ezaki, and Tadayuki Imanaka. "[29] Ribulose-1, 5-bisphosphate carboxylase / oxygenase from Thermococcus kodakaraensis KOD 1." In Hyperthermophilic enzymes Part B. Elsevier, 2001. http://dx.doi.org/10.1016/s0076-6879(01)31070-4.

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Frey, Perry A., and Adrian D. Hegeman. "Decarboxylation and Carboxylation." In Enzymatic Reaction Mechanisms. Oxford University Press, 2007. http://dx.doi.org/10.1093/oso/9780195122589.003.0012.

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Decarboxylation is an essential process in catabolic metabolism of essentially all nutrients that serve as sources of energy in biological cells and organisms. The most widely known biological process leading to decarboxylation is the metabolism of glucose, in which all of the carbon in the molecule is oxidized to carbon dioxide by way of the glycolytic pathway, the pyruvate dehydrogenase complex, and the tricarboxylic acid cycle. The decarboxylation steps take place in thiamine pyrophosphate (TPP)–dependent α-ketoacid dehydrogenase complexes and isocitrate dehydrogenase. The latter enzyme does not require a coenzyme, other than the cosubstrate NAD+. Many other decarboxylations require coenzymes such as pyridoxal-5'-phosphate (PLP) or a pyruvoyl moiety in the peptide chain. Biological carboxylation is the essential process in the fixation of carbon dioxide by plants and of bicarbonate by animals, plants, and bacteria. Carboxylation by enzymes requires the action of biotin or a divalent metal cofactor, and it requires ATP when the carboxylating agent is the bicarbonate ion. The most prevalent enzymatic carboxylation is that of ribulose bisphosphate carboxylase (rubisco), which is responsible for carbon dioxide fixation in plants. The basic chemistry of decarboxylation is illustrated by mechanisms A to D in fig. 8-1. The mechanisms all require some means of accommodation for the electrons from the cleavage of the bond linking the carboxylate group to the α-carbon. In mechanism A, an electron sink at the β-carbon provides a haven for two electrons. Acetoacetate decarboxylase functions by this mechanism (see chap. 1), as well as PLP- and TPP-dependent decarboxylases (see chap. 3). In mechanism B, a leaving group at the β-carbon departs with two electrons. Mevalonate-5-diphosphate decarboxylate functions by mechanism B and is discussed in a later section. In mechanism C, a leaving group replaces the α-carbon and departs with a pair of electrons. A biological example is formate dehydrogenase, in which the leaving group is a hydride that is transferred to NAD+. In mechanism D, a free radical center is created adjacent to the α-carbon and potentiates the homolytic scission of the bond to the carboxylate group. Mechanism D requires secondary electron transfer processes to create the radical center and quench the formyl radical.

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Conference papers on the topic "Ribulose 1-5-bisphosphate carboxylase"

1

Wang, Ruipeng, Zeyu Zhang, Xiaoli Li Li, Lingjun Song, and Huiqiong Li. "Evolution of the Large Subunit of Ribulose-1, 5-Bisphosphate Carboxylase/ Oxygenase Genes in Algae." In 2009 2nd International Conference on Biomedical Engineering and Informatics. IEEE, 2009. http://dx.doi.org/10.1109/bmei.2009.5302275.

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