[Study on the interaction of Cu2Zn2SOD with CoCl2, Co(His)n by spectral and magnetic resonance analysis].
Direct interaction of Cu2Zn2SOD with inorganic metal compound (CoCl2) and organic metal compound [Co(II)(His)n] was studied by ICP, VIS, NMR and measurement of enzyme activity. It has been found that in aqueous solution, there exists a direct interaction of the metal ions of the active center in the metalloenzyme (Cu2Zn2SOD) with external added CoCl2, Co(His)n. As a result, part of the metal ions in metalloenzyme were replaced and the corresponding metalloenzyme derivatives were produced and the catalytic activity of enzyme were affected. Moreover, the interaction of Co(II)(His)n with Cu2Zn2SOD is stronger and quicker, than that of CoCl2 with this enzyme, as well as the Co(II) from Co(II)(His)n is easier to enter the active center of enzyme.
Hu
J
J
Dalian Institute of Chemical Physics, Academia Sinica, 116023 Dalian.
Zheng
X
X
Xu
Y
Y
Cheng
G
G
Zhao
Y
Y
D003035:Cobalt / Q000737:chemistry*; D006639:Histidine / Q000737:chemistry*; D006801:Humans; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D008667:Metalloproteins / Q000737:chemistry*; D008670:Metals / Q000737:chemistry; D011485:Protein Binding; D013482:Superoxide Dismutase / Q000737:chemistry*
D008667:Metalloproteins; D008670:Metals; D003035:Cobalt; D006639:Histidine; D013482:Superoxide Dismutase; C018021:cobaltous chloride