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Literature summary for 1.3.5.1 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
Search for more literature for 1.3.5.1

Inhibitors

Inhibitors Comment Organism Structure
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

Localization Comment Organism GeneOntology No. Textmining
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
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soluble soluble fraction contains FMN, acid-extractable FAD, iron-sulfur protein and c cytochromes of the formate-fumarate reductase electron transport system Wolinella succinogenes
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Metals/Ions

Metals/Ions Comment Organism Structure
Iron the iron-sulfur protein of the electron transport phosphorylation system is the donor for fumarate reductase Wolinella succinogenes

Organism

Organism UniProt Comment Textmining
Wolinella succinogenes
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Renatured (Commentary)

Renatured (Comment) Organism
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

Cofactor Comment Organism Structure
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
iron-sulfur centre the iron-sulfur protein of the electron transport phosphorylation system is the donor for fumarate reductase Wolinella succinogenes

General Information

General Information Comment Organism
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