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Literature summary for 1.14.12.11 extracted from

  • Lin, T.Y.; Werther, T.; Jeoung, J.H.; Dobbek, H.
    Suppression of electron transfer to dioxygen by charge transfer and electron transfer complexes in the FAD-dependent reductase component of toluene dioxygenase (2012), J. Biol. Chem., 287, 38338-38346.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
F1
-

Reaction

Reaction Comment Organism Reaction ID
toluene + NADH + H+ + O2 = (1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+ formation of a stable charge transfer complex between the reduced reductase and NAD+ at the end of the reductive half-reaction, which is substantially less reactive toward dioxygen than the reduced reductase in the absence of NAD+. The nicotinamide ring and the protein matrix shield the reactive C4a position of the isoalloxazine ring and force the tricycle into an atypical planar conformation, both factors disfavoring the reaction of the reduced flavin with dioxygen. A rapid electron transfer from the charge transfer complex to electron acceptors further reduces the risk of unwanted side reactions, there is a short distance between the electron-donating and -accepting cofactors. Attraction between the two proteins is likely mediated by opposite charges at one large patch of the complex interface Pseudomonas putida