Literature summary for 1.13.11.20 extracted from

Attia, A.; Silaghi-Dumitrescu, R.
Nickel-substituted iron-dependent cysteine dioxygenase Implications for the dioxygenation activity of nickel model compounds (2018), Int. J. Quantum Chem., 118, e25564 .

No PubMed abstract available

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ni2+	the optimized structure of the dioxygen-bound active site features an S=2 quintet ground state, with a Ni(III)-superoxo species	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	P21816	-	-

Synonyms

Synonyms	Comment	Organism
CDO1	-	Rattus norvegicus

General Information

General Information	Comment	Organism
metabolism	the O2 activation mechanism suggests the binding of O2 to the metal ion followed by the attack of the distal oxygen atom on the cysteine sulfur. An alternative mechanism entails the attack of the cysteine sulfur on the proximal oxygen atom of the dioxygen moiety to form a persulfenate intermediate without any redox exchange between the metal ion and the O2 ligand. The O2 activation mechanism with a Ni-substituted active site follows the same pattern as native CDOs albeit with much higher energy barriers for the formation of the intermediates. The immediate cleavage of the persulfenate S-O bond in the alternative mechanism suggests that cysteine persulfenate might not be a true intermediate	Rattus norvegicus

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Release 2023.1 (January 2023)