THE REDUCTION OF DISULFIDE BONDS IN PROTEINS AT MERCURY ELECTRODES
Abstract 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 quasi-reversible reduction of a mercury-protein thiolate bonds which are formed from disulfide nonds located in hydrophobic regions of a protein as well as certain sulfhydryl groups and thioethers.