In situ assay of ribulose-1,5-bisphosphate carboxylase/oxygenase in Thiobacillus neapolitanus.
Cells permeabilized with chloroform yielded ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) activities nearly equal to those of cell extracts, thus indicating that both cytoplasmic and carboxysomal RuBisCO are functional in situ. The carboxysomal and cytoplasmic RuBisCO both form the CO2-Mg2(+)-enzyme ternary complex, as evidenced by stabilization with 2-C-carboxy-D-arabinitol-1,5-bisphosphate (CABP), a potent competitive inhibitor of RuBisCO. The data are consistent with the hypothesis that the carboxysome is functional in carbon dioxide fixation.
Cannon
G C
GC
Department of Biological Sciences, Clemson University, South Carolina 29634.
English
R S
RS
Shively
J M
JM
D010940:Plant Proteins; D012273:Ribulose-Bisphosphate Carboxylase / Q000096:biosynthesis* / Q000502:physiology; D013855:Thiobacillus / Q000201:enzymology*
D010940:Plant Proteins; C054765:rca protein, plant; D012273:Ribulose-Bisphosphate Carboxylase