title: The efficiencies of the component steps of oxidative phosphorylation. I. A simple steady state theory.
abstract: Most earlier theoretical work on oxidative phosphorylation has emphasized the application of the formalism of nonequilibrium thermodynamics to the overall process. The resultant mathematical development and interpretation of some experimental data is complicated somewhat by the necessity of treating a system which is incompletely coupled (degree of coupling, q less than 1). Here a simple alternative approach is proposed which can be applied to many studies in the field. In this approach the overall process is broken up into sequential steps so that the product of the efficiencies of the steps is equal to the efficiency of the overall process. Steps of interest for which the degree of coupling may be quite close to unity can be "isolated" by this procedure. This approach results in a simple mathematical formalism emphasizing the power use (or energy use) at each step of the energy transduction process. The efficiencies of the steps of the process can be experimentally evaluated as is shown in the accompanying paper (B.D. Jensen, K. K. Gunter, and T. E. Gunter, 1986, Arch. Biochem. Biophys. 248, 305-323) where measurements are performed as dictated by the assumptions of the current theory. This alternative approach simplifies the analysis of changes induced in the process of oxidative phosphorylation as a result of agents added to the system or of changes in conditions. The locus (or loci) of such changes becomes rapidly apparent if the data is treated as suggested. Furthermore, the mathematical formalism lends itself both to the development of expressions and new experimental approaches which minimize the effects of a decrease in a value of q below unity and also to optimal statistical treatment of the data. As a concrete example of the use of this approach we reinvestigate the question of the equivalence of use of energy from the pH gradient and of the membrane potential in phosphorylation.
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D004563:Electrochemistry; D004579:Electron Transport; D006863:Hydrogen-Ion Concentration; D007473:Ion Channels / Q000502:physiology; D008564:Membrane Potentials; D008928:Mitochondria / Q000378:metabolism; D008954:Models, Biological; D010085:Oxidative Phosphorylation; D006180:Proton-Translocating ATPases / Q000378:metabolism; D011522:Protons; D013816:Thermodynamics
chemical_list: D007473:Ion Channels; D011522:Protons; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases