화학공학소재연구정보센터
Inorganic Chemistry, Vol.45, No.6, 2358-2360, 2006
A nickel superoxide dismutase maquette that reproduces the spectroscopic and functional properties of the metalloenzyme
Described herein is a nickel superoxide dismutase (NiSOD) maquette ([Ni(SODM1)]) based on the first 12 residues from the N-terminal sequence of Streptomyces coelicolor NiSOD. The apopeptide (SODM1) was prepared by standard solid-phase Fmoc peptide synthesis. SODM1 will readily coordinate Ni-II in a 1:1 ratio in slightly basic aqueous sodium phosphate buffer (0.1 M; pH = 7.2) forming a lightly colored beige/pink solution. Unlike NiSOD, which is isolated as a 1:1 mixture of oxidized (Ni-III) and reduced (Ni-II) forms, [Ni(SODM1)] can only be isolated in the Ni-II oxidation state. The UV/vis, X-ray absorption, and CD spectra of [Ni-II(SODM1)] correspond well with those reported for the reduced form of NiSOD. Despite the fact that [Ni-III(SODM1)] is not isolable, [Ni(SODM1)] has an appropriate redox potential to act as an SOD (E-1/2 = 0.70(2) V vs Ag/AgCl) and in fact will catalytically disproportionate > 40 000 equiv of KO2.