Protein disulfide bonds are the links between the sulfur atoms of two cysteine amino acids. All the known life forms appear to make this bond. Most disulfide bonds perform a structural role by stabilizing the tertiary and quaternary structures. Some perform a functional role and can be characterized as either catalytic or allosteric disulfides. Catalytic disulfides/dithiols transfer electrons between proteins, whereas the allosteric bonds control the function of the protein in which they reside when they undergo redox change. There are currently five clear examples of allosteric disulfide bonds and a number of potential allosteric disulfides at various stages of characterization. The features of these bonds and how they control the activity of the respective proteins are discussed. A common aspect of the allosteric disulfides identified to date is that they all link β-strands or β-loops.