Literature summary for 1.13.11.24 extracted from

Li, H.; Wang, X.; Tian, G.; Liu, Y.
Insights into the dioxygen activation and catalytic mechanism of the nickel-containing quercetinase (2018), Catal. Sci. Technol., 8, 2340-2351 .

No PubMed abstract available

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Iron	when the metal cofactor is replaced by an iron ion, the rate-limiting step switches from the Op-Od bond rotation to the collapse of the five-membered ring intermediate, corresponding to a free energy barrier of 30.3 kcal/mol	Streptomyces sp. FLA
Nickel	dioxygen shows two binding modes to the nickel ion, which can convert each other. Due to the overlap between the vacant d orbitals of nickel and the lone pair p orbitals of dioxygen and quercetin, electron transfer occurs from quercetin to dioxygen via the nickel center. Both dioxygen and quercetin can be activated by their binding to the nickel ion. The triplet reactant complex favors the catalytic reaction, and the whole reaction contains four elementary steps. A nonchemical process, the Op-Od bond rotation along the nickel center, is suggested to be rate-limiting with a free energy barrier of 19.9 kcal/mol	Streptomyces sp. FLA

Organism

Organism	UniProt	Comment	Textmining
Streptomyces sp. FLA	A2VA43	-	-

Synonyms

Synonyms	Comment	Organism
QueD	-	Streptomyces sp. FLA

General Information

General Information	Comment	Organism
metabolism	during oxidative ring-cleaving, electron transfer occurs from the quercetin to dioxygen via the nickel ion. Both the dioxygen and substrate are activated by binding to the nickel ion. The catalytic reaction includes the first attack of the Od atom on the quercetin to form the C-O bond, the movement of the coordinated Op atom, the formation of a five-membered heterocyclic ring, and the synergetic cleavage of the O-O bond and C-C bonds. The movement of the coordinated Op atom is the rate-limiting step	Streptomyces sp. FLA

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Release 2023.1 (January 2023)