Literature summary extracted from
Kroeger, A.; Innerhofer, A.
The function of menaquinone, covalently bound FAD and iron-sulfur protein in the electron transport from formate to fumarate of Vibro succinogenes (1976), Eur. J. Biochem., 69, 487-495.
No PubMed abstract available
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
1.3.5.1 |
4-Chloromercuriphenylsulfonate |
inhibits the oxidation of reduced menaquinone by fumarate. Fumarate reductase, measured with reduced benzylviologen as the donor, is not affected |
Wolinella succinogenes |
|
Localization
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
---|
1.3.5.1 |
membrane |
the formate-fumarate reductase electron transport system is localized in the membrane fraction of the bacterium, together with acid-extractable and covalently-bound FAD, menaquinone, iron-sulfur protein and h and c cytochromes |
Wolinella succinogenes |
16020 |
- |
1.3.5.1 |
soluble |
soluble fraction contains FMN, acid-extractable FAD, iron-sulfur protein and c cytochromes of the formate-fumarate reductase electron transport system |
Wolinella succinogenes |
- |
- |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
1.3.5.1 |
Iron |
the iron-sulfur protein of the electron transport phosphorylation system is the donor for fumarate reductase |
Wolinella succinogenes |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.3.5.1 |
Wolinella succinogenes |
- |
- |
- |
Renatured (Commentary)
EC Number |
Renatured (Comment) |
Organism |
---|
1.3.5.1 |
menaquinone is an obligatory redox mediator of formate-fumarate reductase electron transport phosphorylation system. The activity is fully inhibited on the extraction of the menaquinone from the membrane fraction, and is reactivated on reincorporation of menaquinone into the membrane |
Wolinella succinogenes |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.3.5.1 |
FAD |
prosthetic group of fumarate reductase is covalently bound FAD. The specific activity of fumarate reductase is increased to the same extent as the content of the covalently bound FAD when the membrane is fractionated with cholate and ammonium sulfate. The acid-extractable FAD is removed by this procedure |
Wolinella succinogenes |
|
1.3.5.1 |
iron-sulfur centre |
the iron-sulfur protein of the electron transport phosphorylation system is the donor for fumarate reductase |
Wolinella succinogenes |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
1.3.5.1 |
physiological function |
enzyme belongs to a system of electron transport phosphorylation in which formate functions as the donor and fumarate as the terminal acceptor. Menaquinone is an obligatory redox mediator of formate-fumarate reductase electron transport phosphorylation system |
Wolinella succinogenes |