PMID: 79Nov 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.

References

Aug 1, 1972·Proceedings of the National Academy of Sciences of the United States of America·R J Kassner
Apr 1, 1972·Proceedings of the National Academy of Sciences of the United States of America·I Pecht, M Faraggi
Jul 1, 1971·Analytical Biochemistry·E Palecek, Z Pechan
Mar 29, 1967·Journal of the American Chemical Society·T M Bednarski, J Jordan
Oct 1, 1971·FEBS Letters·P D.J. WeitzmanR A. Caldwell

Citations

Dec 31, 1998·Journal of Biochemical and Biophysical Methods·J VidićD Vucelić
Dec 17, 2015·Inorganic Chemistry·Banu KandemirKara L Bren
Mar 1, 1988·European Journal of Biochemistry·J E Frew, H A Hill
Aug 16, 2005·Advances in Colloid and Interface Science·Frieder W SchellerUlla Wollenberger
Oct 16, 2015·The Analyst·Jinming KongTianhe Wang
Aug 17, 1990·European Journal of Biochemistry·A M BondN J Walton

Related Concepts

Cytochrome c Group
Electrode
Respiratory Chain
Hydrogen-Ion Concentration
Mercury
Methemoglobin
Myoglobin
Dioxygen
Pulse Polarography
Potentiometry

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