Nov 18, 1975

Studies on electron transfer between mercury electrode and hemoprotein

Biochimica Et Biophysica Acta
F SchellerE Palecek

Abstract

The electrochemical behaviour of ferricytochrome c, metmyoglobin and methemoglobin was studied using d.c., a.c. and differential pulse polarography, and controlled potential electrolysis. 1. The three hemoproteins yield d.c. polarographic steps, and peaks in differential pulse polarograms, the height of which is proportional to concentration. The charge transfer is influenced by strong adsorption. 2. The concentration dependence of the a.c. polarograms indicates structural changes in the adsorbed molecules. 3. The reduction products of controlled potential electrolysis of metmyoglobin and methemoglobin have absorption spectra identical with the native control samples. The affinity for oxygen and the cooperativity in hemoglobin are not affected by the reaction at the electrode. 4. The charge transfer proceeds via adsorbed, already reduced, molecules to freely diffusible proteins.

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Citations

Mentioned in this Paper

Mercury
Study
Methemoglobin
Dioxygen
Physiologic Pulse
Electron Transport
Adsorption
Cytochrome c Group
Plasma Protein Binding Capacity
Methemoglobin Measurement

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