Diffusion fronts in enzyme-catalysed reactions
نویسندگان
چکیده
In this paper the nature and validity of the mathematical formulation of MichaelisMenten type kinetics for enzyme-catalysed biochemical reactions is studied. Previous work has in the main concentrated on isolated, spatially uniform (well-mixed) reactions. We investigate the effects of substrate input and diffusion on this formulation, in particular, on the nature and validity of the quasi-steady state assumption for diffusion driven fronts. It is shown that provided the Michaelis-Menten constant KM is sufficiently large, then an appropriate quasi-steady state assumption is valid at all points in space and for all times other than in a region which closely tracks the front itself. Moreover, it is shown that this region of shrinks with time.
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