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- W2002076295 abstract "Abstract Recent studies of the disproportionation of H 2 O 2 by Co III -hematoporphyrin IX (Co III HP) show evidence that the reaction proceeds within the coordination sphere of the metal ion. Indeed, as shown now, ligands such as NH 3 , alaninate, adeninate, etc. are competitive inhibitors of the catalyase-like activity of Co III HP. The stability constants, K CoHP(OOH)L CoHP(OOH) , for the complexes of these ligands were estimated and compared with literature values of analog corrin-type complexes. Ligands, like adenosine and adenosine 5′-triphosphate, showed no influence on the catalase-like activity of Co III HP. Obviously, the coordination tendency toward Co III HP of ligands with oxygen as donor atoms is significantly smaller than the one of ligands providing nitrogen as donor. The same behavior had earlier been demonstrated for corrin-type complexes. Additionally, evidence is given for a peroxidase-like activity of Co III HP in the presence of imidazole or derivatives thereof, i.e. these ligands are oxidized. Based on the structure suggested for the active species in the catalase-like reaction, the peroxidase-like reaction can be rationalized: this means, the electron transfer occurs from the coordinated imidazole group through the orbitals of the metal ion to the peroxo species coordinated in the trans position." @default.
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- W2002076295 date "1973-05-01" @default.
- W2002076295 modified "2023-09-26" @default.
- W2002076295 title "Inhibition of the catalase-like activity of cobalt(III)-hematoporphyrin by amino acids, adenine and related ligands Stability of the inhibitor adducts" @default.
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- W2002076295 doi "https://doi.org/10.1016/0022-1902(73)80274-x" @default.
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