The Use of Rotating Disk Voltammetry for the Determination of Homogeneous Small Molecule-Redox Protein Reaction Rates

Document Type

Article

Language

eng

Format of Original

9 p.; 23 cm

Publication Date

7-15-1980

Publisher

Elsevier

Source Publication

Analytical Biochemistry

Source ISSN

0003-2697

Abstract

Rotating disk voltammetry was used in this work to study the rates of reaction of ferricytochrome c with two very strong reductants, methyl and benzyl viologen. The rates of reaction for these reductants were found to be 4.0 × 107 and 5.4 × 107m−1s−1 at 24°C for benzyl and methyl viologen, respectively. The versatility of this method was demonstrated by the ease with which the activation parameters were obtained. The ΔH≠ and ΔS≠ were found to be 4.0 kcal/mol and −10.6 cal/mol-K, respectively, for benzyl viologen. All the observed reaction rates were corrected for coulombic effects by the method of Wherland and Gray, and the electrostatically corrected rate constants were compared with the Marcus and Hopfield theories for electron transfer. The agreement was excellent for the tunneling theory but there were some discrepancies with the absolute Marcus theory. The relative Marcus approach worked quite well and, by taking into account the nonadiabaticity of the electron transfer, reasonable values were obtained for the absolute Marcus theory when realistic values of the self-exchange constants were used.

Comments

Analytical Biochemistry, Vol. 106, No. 1 (July 1980): 269-277. DOI.

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