THE REDUCTION OF DISULFIDE BONDS IN PROTEINS AT MERCURY-ELECTRODES

The adsorption of disulfide containing proteins on mercury and subsequ ent reduction is reviewed. Methods for determining the protein surface excess and number of electroactive disulfide bonds are discussed. Pea ks in up to three potential regions (I, II and III) are observed depen ding on experimental conditions. Peaks in regions I and III have not b een as extensively studied as peak II which is attributed to the rever sible 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.