Download Biomimetic and Bioorganic Chemistry II by F. Vögtle, E. Weber, J. Franke, A. Gärtner, H. Nishide, F.P. PDF

By F. Vögtle, E. Weber, J. Franke, A. Gärtner, H. Nishide, F.P. Schmidtchen, E. Tsuchida, U. Weser

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By the latter procedure low molecular weight reducing agents like ascorbate are removed. In addition, it is advisable to use acetylated or succinylated cytochrome c for the assay, because it is much less susceptible to reductases 160, 161) For routine work using different buffers or solvents, the cytochrome c assay has one advantage which is not present in other indirect assays. The activity of Cu2Zn2superoxide dismutase is dependent on the buffers used. For example, it decreases with increasing ionic strength 162).

A rate constant of 3,8 × 108 Mol-~ × sec 1 is obtained for the model complex using radiolysis. Four coordinated copper in bis cyclo(histidylhistidine) copper(II) complexes have catalytic activities in the same range 256~. The catalytic activity of copper-hystidyl complexes is, however, strongly dependent on the nature of the ligand. Dipeptide complexes of His-X-Cu(lI), where X is phenylalanine, alanine, valine or tyrosine display relatively high superoxide dismutase activity, whereas X-His-Cu(II) complexes are relatively inactive 257).

The rate of oxidation by superoxide is inhibited in the presence of superoxide dismutases 23~. Likewise the autoxidation of catecholamines at alkaline pH-values is diminished 1¢7). Therefore, the interaction between superoxide and catecholamines and its inhibition by SOD is thought not to be a simple chemical reaction 171~Recently, this reaction was investigated in more detail 150~ Whilst adrenalin autoxidation is very specifically inhibited by SOD, the reaction with other catecholamines like noradrenalin or dihydroxyphenylalanine, having no free amino group, is much less specific, Only 20 ~o inhibition by Cu2Zn2superoxide dismutase are observed.

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