Results 191 to 200 of about 29,742 (231)

Mechanism of Action of Ribulose Bisphosphate Carboxylase/Oxygenase

1978
RuBP 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, 1990
INTRODUCTION 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, 1990
Studies 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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Magnetic Resonance Studies on Ribulose Bisphosphate Carboxylase

1978
Experiments 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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Modification of ribulose bisphosphate carboxylase from Rhodospirillumrubrum with tetranitromethane

Biochemical and Biophysical Research Communications, 1979
Abstract 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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Regulation of activation of ribulose bisphosphate carboxylase from Pseudomonasoxalaticus

Biochemical and Biophysical Research Communications, 1978
Abstract 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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Some Mechanistic Aspects of Ribulose Bisphosphate Carboxylase

1984
Water 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.
George H. Lorimer, John Pierce, Steven Gutteridge, John V. Schloss   +3 more
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Comparative Biochemistry of Ribulose Bisphosphate Carboxylase in Higher Plants

1978
The 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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Stoichiometry in the assay of ribulose bisphosphate oxygenase and carboxylase

Analytical Biochemistry, 1982
Abstract 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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Reversible dissociation and conformational stability of dimeric ribulose bisphosphate carboxylase

Biochemistry, 1993
Dimer-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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