Literature summary for 1.14.14.133 extracted from

Kimmich, N.; Das, A.; Sevrioukova, I.; Meharenna, Y.; Sligar, S.G.; Poulos, T.L.
Electron transfer between cytochrome P450cin and its FMN-containing redox partner, cindoxin (2007), J. Biol. Chem., 282, 27006-27011.

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Organism

Organism	UniProt	Comment	Textmining
Citrobacter braakii	Q8VQF6	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1,8-cineole + [reduced flavodoxin] + O2	-	Citrobacter braakii	(1R)-6beta-hydroxycineole + [oxidized flavodoxin] + H2O	-	?

Cofactor

Cofactor	Comment	Organism	Structure
FMN	the FAD/FMN reductase consists of two separate polypeptides where the FMN protein, cindoxin, shuttles electrons between the FAD-containing cindoxin reductase and P450cin. Reaction is highly ionic strength-dependent. The fully reduced hydroquinone is the electron-donating species. Surface interactions are rather different from other P450 proteins	Citrobacter braakii

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Release 2023.1 (January 2023)