Communication
340 - Electrochemical approaches to the study of small molecule-protein reaction rates

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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 [9], where the requirements of low concentrations, small volumes and oxygen exclusion are quite critical. In addition, previous workers [10, 11] 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.

References (11)

  • M.D. Ryan et al.

    Anal. Biochem.

    (1979)
  • A.A.A.M. Brinkman et al.

    J. Electroanal. Chem. Interfacial Electrochem.

    (1967)
  • B.A. Feinberg et al.

    Biochem. Biophys. Res. Commun.

    (1977)
  • M.D. Ryan et al.

    Anal. Chem.

    (1975)
  • L. Hodges et al.

    J. Am. Chem. Soc.

    (1974)
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Cited by (4)

  • Peroxidase enzyme electrodes as nitric oxide biosensors

    2000, Analytica Chimica Acta
    Citation Excerpt :

    However, rapid electron transfer between electrodes and metalloproteins is, in general, difficult to achieve. Thus, many electrochemical studies of redox proteins have made use of small-molecule electrode-active mediators, either free in solution [19,20] or bound to the electrode surface [21,22] to enhance the rate of electron transfer between electrode and protein. This is the approach we have adopted in the design of a peroxidase based electrochemical assay and a peroxidase based biosensor for H2O2.

Presented at the 5th International Symposium on Bioelectrochemistry, 3–8 September 1979, Weimar (D.D.R.).

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