Diffusion fronts in enzyme-catalysed reactions

Graeme P. Boswell, Fordyce A. Davidson

    Research output: Contribution to journalArticlepeer-review

    2 Citations (Scopus)


    In this paper the nature and validity of the mathematical formulation of Michaelis–Menten-type kinetics for enzyme-catalysed biochemical reactions is studied. Previous work has in the main concentrated on isolated, spatially uniform (well-mixed) reactions. 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 are investigated. It is shown that, provided the Michaelis–Menten constant K M is sufficiently large, an appropriate quasi-steady-state assumption is valid at all points in space and for all times other than in a region that closely tracks the front itself. Moreover, it is shown that this region shrinks with time.
    Original languageEnglish
    Pages (from-to)157-169
    Number of pages13
    JournalJournal of Engineering Mathematics
    Issue number2
    Publication statusPublished - 2007


    • Diffusible substrate
    • Michaelis-Menten
    • Open system
    • Quasi-steady state


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