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Literature summary for 7.1.1.12 extracted from

  • Madej, M.; Nasiri, H.; Hilgendorff, N.; Schwalbe, H.; Unden, G.; Lancaster, C.
    Experimental evidence for proton motive force-dependent catalysis by the diheme-containing succinate menaquinone oxidoreductase from the Gram-positive bacterium Bacillus licheniformis (2006), Biochemistry, 45, 15049-15055 .
    View publication on PubMed
Search for more literature for 7.1.1.12

Inhibitors

Inhibitors Comment Organism Structure
2-hydroxy-3-neopentyl-1,4-naphthoquinone competitive Bacillus licheniformis

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane membrane-bound Bacillus licheniformis 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
113000
-
 gel filtration Bacillus licheniformis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
succinate + menaquinone + 2 H+[side 1] Bacillus licheniformis the diheme-containing enzyme exploits the transmembrane electrochemical proton potential DELTAp to support the otherwise thermodynamically unfavorable oxidation of succinate by menaquinone fumarate + menaquinol + 2 H+[side 2]
-
 ?
succinate + menaquinone + 2 H+[side 1] Bacillus licheniformis DSM 13 the diheme-containing enzyme exploits the transmembrane electrochemical proton potential DELTAp to support the otherwise thermodynamically unfavorable oxidation of succinate by menaquinone fumarate + menaquinol + 2 H+[side 2]
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus licheniformis Q65GF3 AND A0A0C5C6P0 AND Q65GF3: cytochrome b558 subunit sdhC, A0A0C5C6P0: flavoprotein subunit sdhA, A0A0C5C686: reductase iron-sulfur protein sdhB
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Bacillus licheniformis DSM 13 Q65GF3 AND A0A0C5C6P0 AND Q65GF3: cytochrome b558 subunit sdhC, A0A0C5C6P0: flavoprotein subunit sdhA, A0A0C5C686: reductase iron-sulfur protein sdhB
-

Purification (Commentary)

Purification (Comment) Organism
purification, reconstitution into proteoliposomes, and functional characterization Bacillus licheniformis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.1
-
 pH and temperature not specified in the publication Bacillus licheniformis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
fumarate + 2,3-dimethyl-1,4-naphthoquinol
-
 Bacillus licheniformis succinate + 2,3-dimethyl-1,4-naphthoquinone
-
 ?
fumarate + 2,3-dimethyl-1,4-naphthoquinol
-
 Bacillus licheniformis DSM 13 succinate + 2,3-dimethyl-1,4-naphthoquinone
-
 ?
succinate + menaquinone + 2 H+[side 1] the diheme-containing enzyme exploits the transmembrane electrochemical proton potential DELTAp to support the otherwise thermodynamically unfavorable oxidation of succinate by menaquinone Bacillus licheniformis fumarate + menaquinol + 2 H+[side 2]
-
 ?
succinate + menaquinone + 2 H+[side 1] the diheme-containing enzyme exploits the transmembrane electrochemical proton potential DELTAp to support the otherwise thermodynamically unfavorable oxidation of succinate by menaquinone Bacillus licheniformis DSM 13 fumarate + menaquinol + 2 H+[side 2]
-
 ?

Subunits

Subunits Comment Organism
oligomer 1 * 23000 (cytochrome b558 subunit sdhC) + 1 * 65000 (flavoprotein subunit sdhA) + 1 * 28000 (reductase iron-sulfur protein sdhB), SDS-PAGE, homotrimeric complex of the heterotrimeric protomer Bacillus licheniformis

Cofactor

Cofactor Comment Organism Structure
heme contains two heme molecules Bacillus licheniformis

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.031
-
 pH and temperature not specified in the publication Bacillus licheniformis 2-hydroxy-3-neopentyl-1,4-naphthoquinone