Results 111 to 120 of about 481 (127)

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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Ribulose bisphosphate carboxylase activity in halophilic Archaebacteria

Archives of Microbiology, 1990
Among 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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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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Modification of histidine at the active site of spinach ribulose bisphosphate carboxylase

Biochemical and Biophysical Research Communications, 1980
Abstract 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.
A K, Saluja, 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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The Active Site of Ribulose Bisphosphate Carboxylase / Oxygenase

1990
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) has attracted a lot of interest due to its central role in the carbon metabolism of plants and photosynthetic microorganisms (for a review see (1)). The dual function of this enzyme, catalyzing the primary steps in both photosynthetic carbon dioxide fixation and photorespiration, makes it a ...
G. Schneider, Y. Lindqvist, T. Lundqvist
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A Perspective on the Biotechnology of Ribulose Bisphosphate Carboxylase/Oxygenase

1989
Publisher Summary This chapter discusses the biotechnology of the photosynthetic enzyme ribulose bisphosphate carboxylase/oxygenase (E.C.4.1.1.39) (Rubisco) because it relates to the possibility of improving photosynthetic yields by suppressing the process of photorespiration in plants.
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Radiochemical assay of ribulose bisphosphate carboxylase

Biochemical Education, 1989
Carl S. Pike, Joseph A. Berry
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Ribulose-bisphosphate carboxylase

1990
Dietmar Schomburg, Margit Salzmann
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RIBULOSE BISPHOSPHATE CARBOXYLASE—AN ENIGMA RESOLVED?

1976
D.A. WALKER, R.Mcc. LILLEY
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