Cleavage of the C–N bond of a peptide group by a copper(II)-peroxide adduct with an η1-coordination mode

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“…This oxidative cleavage of the carboxy-terminal glycine-extended precursor is the basis of the bioactivation of many peptide hormones and neuropeptides. A range of chemical models of PAM has been developed, 17 however, the detailed reaction mechanism of the cleavage of the C-N bond is not clear at present, although crystallographic data have provided considerable insight into part of the mechanism. 18 19 have listed three types of copper dioxygenases: 2,3-dihydroxybenzoate-2,3-dioxygenases that effect 1,2-cleavage of arene-1,2-diols; indole dioxygenases; and quercetin 2,3-dioxygenases (quercetinases), which catalyze the oxygenolysis of 3-hydroxyflavone (12) to the corresponding product (13) as a result of the oxidative cleavage of the heterocyclic ring (Scheme 6).…”

The chemical mechanism of oxidative stress by copper(II) and iron(III) ions in several neurodegenerative disorders

“…When hydrogen peroxide was added to Cu(Me-bdpg)Cl solution (for Me-bdpg, see Fig. 2), the formation of [Cu (bdpg)Cl], not [Cu(dpal)], was detected by ESI-MS [36]. This clearly indicates that Cu(II)-OOH species can cleave the peptide at the C-N bond oxidatively, not hydrolytically, because the hydrolytic cleavage may give Cu(dpal) species from the Cu(Me-bdpg) compound (Scheme 3).…”

Interaction of Cysteine and Nitrilotriacetate with Transition Metal Ions: A Solution Ionophoretic Technique Investigation

“…Their biological importance is attributed to the capabilities of the mercapto groups to undergo various complex formation processes. Fe(III), Cu(II), Ni(II) and Co(II) are well known for their biomedical applications and play essential role in different physiological processes of the body [9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24] . Many transition metal amino acid complexes have considerable biological activity, such as antitumor properties.…”