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On the steady-state assumption and its application to the rotating disk voltammetry of adsorbed enzymes

Article Abstract:

Rotating disk voltammetry is routinely used to study the electrochemically driven enzyme catalysis because of the assumption that the method produces a steady-state system. It is concluded that under typical experimental conditions, steady-state enzyme catalysis is unlikely to occur within electrode-immobilized enzyme layers and that typically sigmoidal rotating disk voltammograms merely reflect a mass transfer steady as opposed to a true steady state of enzyme intermediates at each potential.

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Rates of catalyzed processes in enzymes and other cooperative media

Article Abstract:

The traditional transition stat theory explains catalysis in terms of reduced barriers and result state reaction barriers as intrinsic properties. The considerable rate enhancements exhibited by enzyme-catalyzed reactions with respect to the corresponding processes in solution are interpreted as a consequence of the enhanced coupling of active modes to the reaction coordinate.

Chemical reactions

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Single-molecule Michaelis-Menten equations

Article Abstract:

Models based on the Michaelis-Menten mechanism are presented to account for the experimental observations. The single-molecule Michaelis-Menten equation in the absence of dynamic disorder starting from the differential equations that define both the ensemble-averaged and single-molecule Michaelis-Menten kinetics is discussed.

Enzymatic analysis

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