Literature summary for 1.13.11.39 extracted from

Wang, J.; Chen, J.; Tang, X.; Li, Y.; Zhang, R.; Zhu, L.; Sun, Y.; Zhang, Q.; Wang, W.
Catalytic mechanism for 2,3-dihydroxybiphenyl ring cleavage by nonheme extradiol dioxygenases BphC Insights from QM/MM analysis (2019), J. Phys. Chem. B, 123, 2244-2253 .

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Iron	a quintet state of the 2,3-dihydroxybiphenyl-iron-dioxygen group adducts is the reactive state with a substrate character. The HOO radical species is the reactive oxygen species responsible for the subsequent attack of 2,3-dihydroxybiphenyl	Pseudomonas sp. KKS102

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas sp. KKS102	P17297	-	-

General Information

General Information	Comment	Organism
metabolism	tThe HOO radical species is the reactive oxygen species responsible for the attack of 2,3-dihydroxybiphenyl. The first step in proton-coupled electron transfer is the rate-determining step with a potential energy barrier of 17.2 kcal/mol, close to the experimental value of 14.7 kcal/mol. Residue His194 acts as an acid-base catalyst to deprotonate the hydroxyl group of 2,3-dihydroxybiphenyl at an early stage, then stabilizes the negative charge on the dioxygen group, and finally promotes the semialdehyde product formation as a proton donor	Pseudomonas sp. KKS102

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Release 2023.1 (January 2023)