The importance of the protein in controlling the electrochemistry of heme metalloproteins: methods of calculation and analysis
Program in Gene Function and Expression; Program in Molecular Medicine
The importance of electrostatic effects in determining the free energy of redox reactions in proteins such as cytochromes and iron-sulfur complexes is well established. Several theoretical techniques have been used to analyze how the protein and its environment combine to produce the observed electrochemical midpoints. The free energy of changing the cofactor charge is influenced by the distribution of charges and dipoles in the protein, solvent and ions surrounding the protein, and by the redistribution of these charges and dipoles coupled to the reaction. An outline of a consistent view for calculating these effects will be presented and compared with other theoretical models. Heme redox potentials in yeast cytochrome c and the cytochrome subunit of photosynthetic reaction centers will be calculated to show how these protein structures produce the observed electrochemistry.
DOI of Published Version
Gunner, M.R., Alexov, E., Torres, E., and Lipovaca, S. (1997). The importance of the protein in controlling the electrochemistry of heme metalloproteins: methods of calculation and analysis. Journal of Biological Inorganic Chemistry. 2, 126-134. DOI 10.1007/s007750050116
Journal of Biological Inorganic Chemistry
Gunner MR, Alexov E, Torres EM, Lipovaca S. (1997). The importance of the protein in controlling the electrochemistry of heme metalloproteins: methods of calculation and analysis. Program in Gene Function and Expression Publications. https://doi.org/10.1007/s007750050116. Retrieved from https://escholarship.umassmed.edu/pgfe_pp/227