The redox potentials of electron transfer proteins vary over a wide range, even when the type of redox center is the same. Rees [Proc. Natl. Acad. Sci. USA (1985) 82, 3082-3085] proposed that this variation of redox potential partly reflects the different net charges of the proteins, and he presented a linear correlation between these two properties for 36 proteins. A review of the factors that influence protein redox potentials makes it clear that this linear correlation is fortuitous. The key factors influencing redox potentials are the contributions to the Gibbs energy difference between the two redox states, resulting from bonding interactions at the redox center, electrostatic interactions between the redox-center charge and polar groups within the protein and solvent, and redox-state conformational changes. The relative importance of these terms is likely to vary from protein to protein.
|Number of pages||2|
|Journal||Proceedings of the National Academy of Sciences|
|Publication status||Published - 1986|