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Literature summary for 1.3.5.1 extracted from

  • Condon, C.; Cammack, R.; Patil, D.S.; Owen, P.
    The succinate dehydrogenase of Escherichia coli. Immunochemical resolution and biophysical characterization of a 4-subunit enzyme complex (1985), J. Biol. Chem., 260, 9427-9434.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
15000
-
succinate dehydrogenase, 1 * 71000 + 1 * 26000 + 1 + 17000 + 1 * 15000, immunoprecipitation followed by SDS-PAGE Escherichia coli
26000
-
succinate dehydrogenase, 1 * 71000 + 1 * 26000 + 1 + 17000 + 1 * 15000, immunoprecipitation followed by SDS-PAGE Escherichia coli
71000
-
succinate dehydrogenase, 1 * 71000 + 1 * 26000 + 1 + 17000 + 1 * 15000, immunoprecipitation followed by SDS-PAGE Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
succinate dehydrogenase
-

Subunits

Subunits Comment Organism
tetramer succinate dehydrogenase, 1 * 71000 + 1 * 26000 + 1 + 17000 + 1 * 15000, immunoprecipitation followed by SDS-PAGE Escherichia coli

Cofactor

Cofactor Comment Organism Structure
cytochrome b
-
Escherichia coli
additional information measurement of the redox potentials of the sulfur-centers Escherichia coli
additional information the enzyme contains iron-sulfur centers Escherichia coli