Especially for proteins that contain more than one disulfide bond, it is important that incorrect disulfide bonds become rearranged. This is carried out in the isomerization pathway by the protein DsbC, that acts as a disulfide isomerase. DsbC is a dimer, consisting of two identical 23 kDa subunits and has four cysteine residues in each subunit. One of these cysteines (Cys-98) attacks an incorrect disulfide in a misfolded protein and a mixed disulfide is formed between DsbC and this protein. Next, the attack of a second cysteine residue results in the forming of a more stable disulfide in the refolded protein. This may be a cysteine residue either from the earlier misfolded protein or one from DsbC. In the last case, DsbC becomes oxidized and has to be reduced in order to play another catalytic role. There is also a second isomerase that can reorganize incorrect disulfide bonds. This protein is called DsbG and it is also a dimer that serves as a chaperone. In order to fulfil their role as isomerases, DsbC and DsbG need to be kept in a reduced state. This is carried out by DsbD, which has to be reduced itself to be functional. Thioredoxin, which itself is reduced by thioredoxin reductase and NADPH, ensures the reduction of the DsbD protein.