Electrostatic interactions in the reaction mechanism of bovine erythrocyte superoxide dismutase.

摘要: The activity of the copper- and zinc-containing superoxide dismutase decreased with increasing ionic strength. Modification lysine residues by acetylation or succinylation inverted effect strength, whereas modification arginine phenylglyoxal did not. These results were noted in both photochemical pulse-radiolysis assays. It appears that interaction O2- anionic enzyme is assisted positive charge on residues, presumably those close to active site. By criterion responsiveness residue site does not appear provide electrostatic facilitation catalytic process. Elimination epsilon-amino groups raising pH suppressed same extent as elimination these charges acetylation. Activity was similarly covalent ionization indicating important for process even though its responsive changes strength solution.