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Comparative Biochemistry of Ribulose Bisphosphate Carboxylase in Higher Plants
1978The agronomically important aspects of the comparative biochemistry of RuBP carboxylase are locating a natural enzyme, creating a mutant enzyme, or identifying compounds which differentially alter the enzyme so as to allow CO2 to be fixed more efficiently or O2 to be fixed less efficiently.
William L. Ogren, Larry D. Hunt
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Some Mechanistic Aspects of Ribulose Bisphosphate Carboxylase
1984Water is involved in the carboxylase reaction in 2 distinct ways (Fig 1.) Besides its stoichiometric involvement, it hydrates both substrates. While carbon dioxide has long been recognised as the active species, no information is yet available on how the enzyme handles the geM-diol form of RuBP.
John V. Schloss +3 more
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The Relationship Between Ribulose Bisphosphate Carboxylase Concentration and Photosynthesis [PDF]
, 1981 Ribulose 1, 5-bisphosphate carboxylase (RuBPCase) has a central role in the C and N economy of many crop plants. In C3 plants, RuBPCase catalyzes the primary rate-limiting step in CO2 fixation (Jensen and Bahr, 1977; Bahr and Steffens, this volume). RuBPCase also functions as a storage protein and is rapidly degraded during leaf senescence (Friedrich ...
R. C. Huffaker, James W. Friedrich
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Ribulose bisphosphate carboxylase—oxygenase: its role in photosynthesis
Philosophical Transactions of the Royal Society of London. B, Biological Sciences, 1986Synthesis of triose phosphate by the chloroplast requires three substrates: light, CO2and orthophosphate (Pi). In the response of the rate of carbon assimilation to the concentration of CO2, the kinetic properties of RuBP carboxylase-oxygenase (Rubisco) constitute the main limitation at low CO2concentrations, while at higher concentrations of CO2the ...
Mirta N. Sivak +2 more
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Crystal structure of the active site of ribulose-bisphosphate carboxylase
Nature, 1989Ribulose-bisphosphate carboxylase catalyses the key carboxylation reaction of photosynthetic carbon fixation, but also the competing oxygenase reaction of photorespiration. The structure of the active site of ribulose-bisphosphate carboxylase described here should provide a rational basis for attempts to improve the efficiency of the enzyme by genetic ...
Ylva Lindqvist +6 more
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Immunocytochemical detection of ribulose bisphosphate carboxylase in capsicum plastids
Biology of the Cell, 1988SUMMARYRibulose bisphosphate carboxylase (RUBPCase) was localized by fluorescence and gold immunocytochemistry in Capsicum fruits. Chloroplasts of the green fruit are heavily labelled. A positive staining is also obtained with chromoplasts of the ripe rad fruit, but gold labelling is fainter.
Jean-Pierre Carde +2 more
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Modification of histidine at the active site of spinach ribulose bisphosphate carboxylase
Biochemical and Biophysical Research Communications, 1980Abstract Ribulose 1,5-bisphosphate carboxylase from spinach was rapidly inactivated by diethylpyrocarbonate (DEP) at pH 7.0 and 30°C. The inactivation showed saturation kinetics with a half-inactivation time at saturating DEP equal to 0.1 minutes and KDEP = 7.4 mM.
Bruce A. McFadden, Ashok K. Saluja
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Radiochemical assay of ribulose bisphosphate carboxylase
Biochemical Education, 1989Carl S. Pike, Joseph A. Berry
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Regulation of the Activity of Ribulose Bisphosphate Carboxylase by Light and CO2
1990Ribulose 1,5-bisphosphate (RuBP) carboxylase (Rubisco) is known as being a light-regulated enzyme.
Juta Viil, Tiit Pärnik
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