Studies on electron transfer between mercury electrode and hemoprotein.
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.
D001665:Binding Sites; D003574:Cytochrome c Group; D004566:Electrodes; D004579:Electron Transport; D006863:Hydrogen-Ion Concentration; D008628:Mercury; D008706:Methemoglobin; D009211:Myoglobin; D010100:Oxygen / Q000097:blood; D011048:Polarography; D011199:Potentiometry; D011485:Protein Binding; D013053:Spectrophotometry
D003574:Cytochrome c Group; D009211:Myoglobin; D008706:Methemoglobin; D008628:Mercury; D010100:Oxygen