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Literature summary for 1.3.5.1 extracted from

  • Haegerhaell, C.; Sled, V.; Hederstedt, L.; Ohnishi, T.
    The trinuclear iron-sulfur cluster S3 in Bacillus subtilis succinate:menaquinone reductase; effects of a mutation in the putative cluster ligation motif on enzyme activity and EPR properties (1995), Biochim. Biophys. Acta, 1229, 356-362.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
S214C/Q215G substitution in the IP subunit, mutant is enzymatically impaired and less stable than wild-type Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
2-(n-heptyl)-4-hydroxy-quinoline N-oxide
-
 Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
 succinate dehydrogenase
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
succinate + 2,3-dimethoxy-5-methyl-6-(3,7-dimethyl-2,6-octadienyl)-1,4-benzoquinone
-
 Bacillus subtilis fumarate + 2,3-dimethoxy-5-methyl-6-(3,7-dimethyl-2,6-octadienyl)-1,4-benzoquinol
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
additional information analysis of the functional role of the trinuclear cluster S3 in the enzyme by introducing a fourth cysteine residue into the putative ligation motif to that cluster Bacillus subtilis
additional information the enzyme contains iron-sulfur centers Bacillus subtilis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0004
-
 2-(n-heptyl)-4-hydroxy-quinoline N-oxide inhibitor of the activity of mutant and wild-type enzyme Bacillus subtilis