A method aimed at assessing the functional consequences of the supramolecular organization of the respiratory...

A steadily increasing number of physiological, biochemical, and structural studies have provided a growing support to the notion that the respiratory electron transfer chain may contain supra-molecular edifices made of the assembly of some, if not all, of its individual links. This structure, usually referred to as the solid state model-in comparison to the liquid state model in which the electron transfer reactions between the membrane bound enzymes are diffusion controlled-is seen as conferring specific kinetic properties to the chain and thus as being highly relevant from a functional point of view. Although the assumption that structural changes are mirrored by functional adjustment is undoubtedly legitimate, experimental evidences supporting it remain scarce. Here we review a recent methodological development aimed at tackling the functional relevance of the supramolecular organization of the respiratory electron transfer chain in intact cells.