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 ...
Kris Purohit, Bruce A. McFadden
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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.
R. C. Valentine, K. Andersen, W. King
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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 [PDF]
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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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.
Henry M. Miziorko, M. Daniel Lane
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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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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.
Rose Ann Cattolico, Scott M. Newman
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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.
Peter D. Robison, F. Robert Tabita
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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.
Bruce A. McFadden+2 more
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The Active Site of Ribulose Bisphosphate Carboxylase / Oxygenase
1990Ribulose-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 ...
Gunter Schneider+2 more
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