Results 101 to 110 of about 481 (127)
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Stoichiometry in the assay of ribulose bisphosphate oxygenase and carboxylase
Analytical Biochemistry, 1982Abstract Complete stoichiometry of the reaction catalyzed by ribulose 1,5-bisphosphate (RuBP) oxygenase from spinach and Rhodospirillum rubrum has been determined. Before initiation and after termination, RuBP has been measured either by release of equimolar orthophosphate at 25°C in the presence of 1 n NaOH or by complete carboxylation using 14CO2
K, Purohit, B A, McFadden, A, Saluja
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Chemosynthetic, Photosynthetic, and Cyanobacterial Ribulose Bisphosphate Carboxylase
1978There are compelling reasons to believe that the initial atmosphere of the earth after its formation about 4.7 × 109 years ago was a reducing one consisting chiefly of methane, ammonia, water, and hydrogen (1). In the last two decades considerable research has been described in which numerous organic precursors of biopolymers have been synthesized ...
B A, McFadden, K, Purohit
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Catalytic Mutants of Ribulose Bisphosphate Carboxylase/Oxygenase
1978Ribulose bisphosphate (RuBP) carboxylase/oxygenase, which may be the most abundant protein in nature, is recognized as the cardinal enzyme catalyzing carbon dioxide fixation yielding energy-rich photosynthate.
K, Andersen, W, King, R C, Valentine
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Mechanism of Action of Ribulose Bisphosphate Carboxylase/Oxygenase
1978RuBP carboxylase-oxygenase appears to catalyze carboxylation and oxygenation by homologous mechanisms. A common binding site exists on the enzyme for the acceptor substrate, RuBP. A mechanism is proposed whereby RuBP is isomerized, and a carbanion is generated at C2.
M D, Lane, H M, Miziorko
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Chaperone Function: The Assembly of Ribulose Bisphosphate Carboxylase-Oxygenase
Annual Review of Cell Biology, 1990INTRODUCTION 126 TI-I~ MOLECULAR CH PERO~ CONCEPT 126 The Problem of lnteractive Surfaces 127 Assisted Self-Assembly 129 The Chaperonins 129 Tim IMPORa’ANCE OF RUBISCO 131 Properties 131 Structure 132 Synthesis 133 THE PLASTID CHAPERONIN 134 Discovery 134 Role in Rubisco Assembly by Chloroplasts 134 SYNTHESIS AND ASSEMBLY OF ...
A A, Gatenby, R J, Ellis
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Ribulose bisphosphate carboxylase in algae: synthesis, enzymology and evolution
Photosynthesis Research, 1990Studies demonstrating differences in chloroplast structure and biochemistry have been used to formulate hypotheses concerning the origin of algal plastids. Genetic and biochemical experiments indicate that significant variation occurs in ribulose-1,5-bisphosphate carboxylase (Rubisco) when supertaxa of eukaryotic algae are compared.
S M, Newman, R A, Cattolico
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Carboxysomes and Ribulose Bisphosphate Carboxylase/Oxygenase
1988Publisher Summary This chapter focuses on recent advances made in the knowledge of the occurrence, composition, properties, and possible functions of carboxysomes. It also discusses the rapidly expanding field of research on Ribulose 1, 5-bisphosphate carboxylase/oxygenase (RuBisCO) enzymes.
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Regulation of activation of ribulose bisphosphate carboxylase from Pseudomonasoxalaticus
Biochemical and Biophysical Research Communications, 1978Abstract 6-phosphogluconate, potentiated activation of ribulose bisphosphate carboxylase from Pseudomonas oxalaticus whereas fructose-1,6-bisphosphate inhibited activation and fructose-6-phosphate had no effect. The presence of 1 mM 6-phosphogluconate during activation reduced the Kact for Mg2+ from 1.4 mM to approximately 0.2 mM.
V B, Lawlis, G L, Gordon, B A, McFadden
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Modification of ribulose bisphosphate carboxylase from Rhodospirillumrubrum with tetranitromethane
Biochemical and Biophysical Research Communications, 1979Abstract Ribulose bisphosphate carboxylase from Rhodospirillum rubrum is inactivated by low concentrations of tetranitromethane. Addition of the substrate ribulose 1,5-bisphosphate and preincubation with Mg+2 and HCO 3 − both protect against inactivation.
P D, Robison, F R, Tabita
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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.
W L, Ogren, L D, Hunt
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