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Published August 15, 1980 | public
Journal Article

Experimental Evaluation of the Effective Dielectric Constant of Proteins

Abstract

Chemical modifications that alter the net charge of residues in reduction-oxidation proteins influence the redox potential of the protein by changing the electrostatic potential at the redox center. If the locations of the modified charges are known, the shift in redox potential may be used to determine the effective dielectric constant for the interactions between the redox center and modified residues. From the shift in redox potential upon charge neutralization of specific lysines in the hemoprotein cytochrome c, an effective dielectric constant of approximately 50 is calculated for the electrostatic interaction between the modified lysines and heme iron in the native protein.

Additional Information

© 1979 Academic Press Inc. (London) Ltd. Received 25 March 1980. We thank W. N. Lipscomb for advice and encouragement. This work was supported by National Institutes of Health grant GM06920.

Additional details

Created:
August 19, 2023
Modified:
October 20, 2023