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Literature summary extracted from

  • Hederstedt, L.
    Succinate:quinone oxidoreductase in the bacteria Paracoccus denitrificans and Bacillus subtilis (2002), Biochim. Biophys. Acta, 1553, 74-83.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.5.1 description of succinate dehydrogenase operon Paracoccus denitrificans
1.3.5.1 description of succinate dehydrogenase operon Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
1.3.5.1 G168D enzyme not assembled, properties of heme bP and heme bD seem normal Bacillus subtilis
1.3.5.1 H113L enzyme not assembled Bacillus subtilis
1.3.5.1 H113M assembled enzyme, low enzyme activity, altered properties of heme bD compared to wild-type Bacillus subtilis
1.3.5.1 H113Y enzyme not assembled, contains heme Bacillus subtilis
1.3.5.1 H13Y assembles enzyme with about 50% of normal activity, alters properties of heme bP and heme bD compared to wild-type, the isolated enzyme is not stable in the presence of succinate Bacillus subtilis
1.3.5.1 H155L assembled enzyme, the enzyme has some activity but apparently is unstable Bacillus subtilis
1.3.5.1 H155Y enzyme not assembled, contains heme Bacillus subtilis
1.3.5.1 H28L assembles succinate dehydrogenase, active succinate dehydrogenase but inactive succinate: quinone reductase, contains heme bP but lacks low potential heme Bacillus subtilis
1.3.5.1 H28Y enzyme not assembled, contains heme Bacillus subtilis
1.3.5.1 H47Y assembles fully active enzyme Bacillus subtilis
1.3.5.1 H70L enzyme not assembled Bacillus subtilis
1.3.5.1 H70Y enzyme not assembled Bacillus subtilis
1.3.5.1 H70Y/Y73S assembled enzyme, enzyme activity is 30% of normal Bacillus subtilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.5.1 2-(n-heptyl)-4-hydroxy-quinoline N-oxide potent inhibitor that affects both reduction and oxidation of quinone, the inhibitor binds close to heme bD Bacillus subtilis
1.3.5.1 2-Thenoyltrifluoroacetone
-
 Paracoccus denitrificans
1.3.5.1 carboxin not inhibitory Bacillus subtilis
1.3.5.1 carboxin interferes with electron transfer from the 3Fe-4S center to quinone, carboxin may bind to a quinone-binding site the Qp site, close to the 3Fe-4S center, amino acids involved in binding carboxin: a histidine residue in the B subunit and an aspartate residue in the D subunit Paracoccus denitrificans

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.5.1 cytoplasmic membrane
-
 Paracoccus denitrificans
-
-
1.3.5.1 cytoplasmic membrane
-
 Bacillus subtilis
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.5.1 additional information Paracoccus denitrificans the enzyme has the function to oxidize succinate to fumarate, as part of the Krebs' cycle and directly couples this to the reduction of quinone in the membrane, quinol is then oxidized by the respiratory chain ?
-
 ?
1.3.5.1 additional information Bacillus subtilis the enzyme has the function to oxidize succinate to fumarate, as part of the Krebs' cycle and directly couples this to the reduction of quinone in the membrane, quinol is then oxidized by the respiratory chain ?
-
 ?
1.3.5.1 succinate + ubiquinone Paracoccus denitrificans
-
 fumarate + ubiquinol
-
 ?
1.3.5.1 succinate + ubiquinone Bacillus subtilis
-
 fumarate + ubiquinol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.5.1 Bacillus subtilis
-
 succinate dehydrogenase
-
1.3.5.1 Paracoccus denitrificans
-
 succinate dehydrogenase
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.5.1 additional information the enzyme has the function to oxidize succinate to fumarate, as part of the Krebs' cycle and directly couples this to the reduction of quinone in the membrane, quinol is then oxidized by the respiratory chain Paracoccus denitrificans ?
-
 ?
1.3.5.1 additional information the enzyme has the function to oxidize succinate to fumarate, as part of the Krebs' cycle and directly couples this to the reduction of quinone in the membrane, quinol is then oxidized by the respiratory chain Bacillus subtilis ?
-
 ?
1.3.5.1 succinate + ubiquinone
-
 Paracoccus denitrificans fumarate + ubiquinol
-
 ?
1.3.5.1 succinate + ubiquinone
-
 Bacillus subtilis fumarate + ubiquinol
-
 ?
1.3.5.1 succinate + ubiquinone electron acceptor: menaquinone Bacillus subtilis fumarate + ubiquinol
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.5.1 tetramer
-
 Paracoccus denitrificans
1.3.5.1 trimer
-
 Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.5.1 FAD
-
 Paracoccus denitrificans
1.3.5.1 FAD
-
 Bacillus subtilis
1.3.5.1 heme b
-
 Paracoccus denitrificans
1.3.5.1 heme b heme bP und heme bD Bacillus subtilis
1.3.5.1 additional information the enzyme contains iron-sulfur centers Paracoccus denitrificans
1.3.5.1 additional information the enzyme contains iron-sulfur centers Bacillus subtilis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.3.5.1 0.0002
-
 2-(n-heptyl)-4-hydroxy-quinoline N-oxide
-
 Bacillus subtilis