A paper published!(論文発表)


Copper-zinc superoxide dismutase (CuZnSOD) is an enzyme that catalyzes the disproportionation of superoxide and is conserved from bacteria to humans. It binds copper and zinc ions and also forms an intramolecular disulfide bond. We have previously shown that the intramolecular disulfide bond plays a critical role in both structural stability and enzymatic activity and is therefore highly conserved in CuZnSOD. However, a close examination of CuZnSODs in the NCBI database revealed that some CuZnSODs in Paenibacillus (Gram-positive bacteria), named PaSOD, lack cysteines and are expected to have a novel domain structure. Therefore, in this study, we investigated the expression, activity and structure of PaSOD and discussed the physiological significance of the lack of cysteines in CuZnSOD in Paenibacillus. Please click here for more details.