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Effects of Nonpolar Environments on the Redox Potentials of Heme Complexes
Author(s) -
Richard J. Kassner
Publication year - 1972
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.69.8.2263
Subject(s) - redox , heme , chemistry , hemeprotein , reduction potential , aqueous solution , inorganic chemistry , biochemistry , organic chemistry , enzyme
A method has been described for measurement of the oxidation-reduction potentials of redox couples in nonaqueous solutions. This method has been applied to a study of the effect of a nonpolar environment on the redox potential of a heme complex. A positive potential difference of some 300 mV is observed for the measured redox potentials by comparison with reported values for the corresponding heme complex in aqueous solution. The proposal is made that the redox potentials of many high-potential cytochromes may be accounted for by a local heme environment of low-dielectric constant, characteristic of nonpolar amino-acid side chains, and that this factor may play a dominant role in the determination of the oxidation-reduction properties of these proteins.

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