Literature summary for 1.2.7.B2 extracted from

Liao, R.Z.; Yu, J.G.; Himo, F.
Tungsten-dependent formaldehyde ferredoxin oxidoreductase: reaction mechanism from quantum chemical calculations (2011), J. Inorg. Biochem., 105, 927-936.

Search for more literature for 1.2.7.B2

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Tungsten	tungsten-dependent enzyme. A mechanism is proposed in which the formaldehyde substrate binds directly to the tungsten ion. W(VI)=O then performs a nucleophilic attack on the formaldehyde carbon to form a tetrahedral intermediate. In the second step, which is calculated to be rate limiting, a proton is transferred to the second-shell Glu308 residue, coupled with a two-electron reduction of the tungsten ion	Pyrococcus furiosus

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus furiosus	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
formaldehyde + H2O + 2 oxidized ferredoxin = formate + 2 H+ + 2 reduced ferredoxin	a mechanism is proposed in which the formaldehyde substrate binds directly to the tungsten ion. W(VI)=O then performs a nucleophilic attack on the formaldehyde carbon to form a tetrahedral intermediate. In the second step, which is calculated to be rate limiting, a proton is transferred to the second-shell Glu308 residue, coupled with a two-electron reduction of the tungsten ion	Pyrococcus furiosus	a

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)