Characterization of the ribulosebisphosphate carboxylase-carbon dioxide-divalent cation-carboxypentitol bisphosphate complex.
Ribulosebisphosphate carboxylase forms a stable quaternary complex with CO2, divalent cation, and carboxypentitol bisphosphate. Incorporation of nonexchangeable CO2 into the complex requires the presence of a divalent cation. MG2+, Mn2+, or Co2+ supports stoichiometric binding of CO2 activator. When the quaternary complex is formed in the presence of saturating CO2, stoichiometric amounts of cation are bound in a nonexchangeable fashion. Incorporation of Mn2+ into an enzyme-CO2-Mn2+-carboxypentitol bisphosphate complex permitted investigation of cation environment by electron spin resonance (ESR) techniques. Measurements at 9 and 35 GHz suggest rhombic distortion of the coordination sphere of bound Mn2+. A complex inner sphere liganding of the cation bound in the quaternary complex would account for both the ESR spectra and the marked stability of the complex with respect to cation exchange.
D001665:Binding Sites; D002245:Carbon Dioxide; D002262:Carboxy-Lyases / Q000378:metabolism; D003035:Cobalt; D003300:Copper; D004578:Electron Spin Resonance Spectroscopy; D004789:Enzyme Activation; D007700:Kinetics; D008274:Magnesium; D008345:Manganese; D010428:Pentosephosphates; D010944:Plants / Q000201:enzymology; D011485:Protein Binding; D012273:Ribulose-Bisphosphate Carboxylase / Q000378:metabolism*
D010428:Pentosephosphates; C024935:carboxypentitol bisphosphate; D002245:Carbon Dioxide; D003035:Cobalt; D008345:Manganese; D003300:Copper; D002262:Carboxy-Lyases; D012273:Ribulose-Bisphosphate Carboxylase; D008274:Magnesium