Literature summary for 1.14.14.9 extracted from

Visitsatthawong, S.; Chenprakhon, P.; Chaiyen, P.; Surawatanawong, P.
Mechanism of oxygen activation in a flavin-dependent monooxygenase A nearly barrierless formation of C4a-hydroperoxyflavin via proton-coupled electron transfer (2015), J. Am. Chem. Soc., 137, 9363-9374 .

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Organism

Organism	UniProt	Comment	Textmining
Acinetobacter baumannii	Q6Q272	oxygenase component C2	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the protonation of dioxygen by residue His396 of hte oxygenase component via a proton-coupled electron transfer mechanism is the key step in the formation of the triplet diradical complex of flavin semiquinone and the hydroperoxide radical. The complex undergoes intersystem crossing to form the open-shell singlet diradical complex before it forms the closed-shell singlet C4a-hydroperoxyflavin intermediate. The formation of C4a-hydroperoxyflavin is nearly barrierless. The enthalpy of activation for the formation of C4a-hydroperoxyflavin is only 1.4 kcal/mol and the formation is fast. Ser171 is the key residue that stabilizes C4a-hydroperoxyflavin by accepting a hydrogen bond from the H(N5) of the isoalloxazine ring. Both Ser171 and Trp112 facilitate H2O2 elimination by donating hydrogen bonds to the proximal oxygen of the hydroperoxide moiety during the proton transfer	Acinetobacter baumannii	?	-	?

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Release 2023.1 (January 2023)