Perturbation of molecular species distribution in steady states supported by a flow of energy. Models analogous to Ca2(+)-dependent ATPase and phosphorylase b.
When an allosteric macromolecular system is capable of existing in two conformations, both of which may be converted into energy-storing forms by the binding of a substrate or by the absorption of radiant energy, then a kinetic process may occur, such as an enzymic conversion of the substrate into products, which liberates energy and selectively depletes one or more of the forms of the macromolecule. Upon a continuous supply of energy, a steady state, or pseudoequilibrium, is reached during which the selective depletion of molecular species results effectively in a directional flow of energy through the system. This perturbs the distribution of the various molecular species. This effect may simulate both positive and negative binding cooperativity, and mimic the presence of multiple binding sites with different affinities even in monomeric, monovalent systems. Specific model systems are presented analogous to the transport of Ca2+ by sarcoplasmic reticulum and the allosteric behavior of phosphorylase b.
Bucci
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E
Department of Biochemistry, University of Maryland Medical School, Baltimore 21201.
Steiner
R F
RF
D000494:Allosteric Regulation; D001665:Binding Sites; D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D007700:Kinetics; D008024:Ligands; D008433:Mathematics; D008962:Models, Theoretical; D010763:Phosphorylase b / Q000378:metabolism*; D011487:Protein Conformation
D008024:Ligands; D010763:Phosphorylase b; D000252:Calcium-Transporting ATPases