Results 131 to 140 of about 40,127 (172)
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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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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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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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Ribulose bisphosphate carboxylase activity in halophilic Archaebacteria
Archives of Microbiology, 1990Among the several strains of halobacteria grown heterotrophically, ribulose bisphosphate carboxylase activity was detected in those which accumulate poly (β-hydroxybutyrate), viz. Haloferax mediterranei, Haloferax volcanii and Halobacterium marismortui. In H.
Wijaya Altekar, Rema Rajagopalan
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Magnetic Resonance Studies on Ribulose Bisphosphate Carboxylase
1978Experiments have been initiated aimed at elucidating the role of the divalent cation required in the RuBP carboxylase-catalyzed reaction. Metal ion is clearly required for activation of the enzyme. However, there is some question concerning an additional role for metal in the catalytic process.
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Reversible dissociation and conformational stability of dimeric ribulose bisphosphate carboxylase
Biochemistry, 1993Dimer-monomer dissociation of ribulosebisphosphate carboxylase/oxygenase from Rhodospirillum rubrum was investigated using hydrostatic pressure in the range 1-2 kbar to promote dissociation. Intrinsic fluorescence emission and polarization, along with the polarization of the fluorescence of single-labeled AEDANS conjugates, were used to follow the ...
L, Erijman, G H, Lorimer, G, Weber
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