Results 221 to 230 of about 25,095 (239)
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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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Phosphoglycolate production catalyzed by ribulose diphosphate carboxylase
Biochemical and Biophysical Research Communications, 1971Abstract An oxygen-dependent production of phosphoglycolate is catalyzed by purified soybean ribulose diphosphate carboxylase and by crude extracts of soybean and corn leaves. It is suggested that the phosphoglycolate produced in this reaction is the source of glycolate metabolized in photorespiration.
G, Bowes, W L, Ogren, R H, Hageman
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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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Ribulose diphosphate carboxylase
Archives of Biochemistry and Biophysics, 1970W.R. Andersen +2 more
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1966
Publisher Summary The enzymatic procedure described is based on the use of L-ribulokinase from an L-ribulose 5-phosphate 4-epimeraseless mutant of Escherichia coli . The use of this mutant obviates the need to purify L-ribulokinase to obtain a product free from D-xylulose 5-phosphate and D-ribulose 5-phosphate.
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Publisher Summary The enzymatic procedure described is based on the use of L-ribulokinase from an L-ribulose 5-phosphate 4-epimeraseless mutant of Escherichia coli . The use of this mutant obviates the need to purify L-ribulokinase to obtain a product free from D-xylulose 5-phosphate and D-ribulose 5-phosphate.
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1966
Publisher Summary This chapter reveals that the D-Ribulose 5-phosphate is prepared by the triphosphopyridine nucleotide (TPN)-coupled enzymatic oxidation of D-glueonate 6-phosphate followed by treatment with charcoal and precipitation of the phosphorylated product as barium or lithium salt.
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Publisher Summary This chapter reveals that the D-Ribulose 5-phosphate is prepared by the triphosphopyridine nucleotide (TPN)-coupled enzymatic oxidation of D-glueonate 6-phosphate followed by treatment with charcoal and precipitation of the phosphorylated product as barium or lithium salt.
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5 Ribulose-1,5-Diphosphate Carboxylase
1972Publisher Summary This chapter discusses the molecular properties and catalytic process of ribulose-1,5-diphosphate carboxylase. The identification by Calvin and his colleagues of phosphoglyceric acid as the first stable radioactive product formed during a brief exposure of algae to 14CO2 led ultimately to the discovery that the carboxylation of ...
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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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