Mechanisms and rate equations for dissociating systems.
The results presented in the previous paper (Boeker, E.A. (1978), Biochemistry 17 (preceding paper in this issue) indicate that the dissociation of the decamer of arginine decarboxylase of Escherichia coli B is enhanced by Na+ and retarded by H+. In this system, substances which increase the rate of dissociation can be treated kinetically either as substrates or activators, and substances which retard dissociation can be treated as products or inhibitors. In addition, the events needed for dissociation can occur in an ordered or a random sequence, and the dissociation itself, from a decamer to five dimers, can be a sequential or a concerted process. In order to provide a framework for the experimental results, mechanisms for the dissociation of arginine decarboxylase that take all of these factors into account are described. In addition, it is shown that the usual methods of steady-state kinetics can be applied to these systems when true initial rates are measured; rate equations are presented for each mechanism. The results can be used for any dissociating of three or more subunits and will describe the dissociation of a dimer under certain conditions.
D001120:Arginine; D002262:Carboxy-Lyases; D004228:Dithionitrobenzoic Acid; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008956:Models, Chemical; D008970:Molecular Weight; D010455:Peptides; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins; D012964:Sodium
D010455:Peptides; D011506:Proteins; D001120:Arginine; D004228:Dithionitrobenzoic Acid; D012964:Sodium; D002262:Carboxy-Lyases