The reduction of disulfide bonds in proteins at mercury electrodes

The adsorption of disulfide containing proteins on mercury and subsequent reduction is reviewed. Methods for determining the protein surface excess and number of electroactive disulfide bonds are discussed. Peaks in up to three potential regions (I, II and III) are observed depending on experimental conditions. Peaks in regions I and III have not been as extensively studied as peak II which is attributed to the reversible or quasireversible reduction of a mercury-protein thiolate bonds which are formed from disulfide bonds located in hydrophobic regions of a protein as well as certain sulfhydryl groups and thioethers. (C) 1997 Elsevier Science S.A.