Electrochemical Approaches to the Study of Small Molecule-Protein Reaction Rates
Bioelectrochemistry and Bioenergetics, Vol. 7, No. 3 (September 1980): 587-594. DOI.
Abstract
The reduction kinetics of small molecule-protein reactions can be studied quite efficiently by the use of pulse polarography and differential pulse polarography. These results were obtained quite easily for relatively low concentrations of the mediator. It is only for differential pulse polarography that there is an absolute increase in the sensitivity when compared to chronoamperometry. This approach has been recently applied in our laboratory to low potential proteins such as spinach ferrodoxin, where the requirements of low concentrations, small volumes and oxygen exclusion are quite critical. In addition, previous workers have shown that pulse and differential pulse polarography can be applied to stationary electrodes, which would greatly expand these approaches for small molecule-protein reaction studies.