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Literature summary extracted from

  • Ziegler, D.; Rieske, J.S.
    Preparation and properties of succinate dehydrogenase-coenzyme Q reductase (Complex II) (1967), Methods Enzymol., 10, 231-235.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.5.1 2-Thenoyltrifluoroacetone 97% inhibition at 0.1 mM Bos taurus
1.3.5.1 4-Chloromercuriphenyl sulfonate
-
 Bos taurus
1.3.5.1 CN-
-
 Bos taurus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.3.5.1 Fe
-
 Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
1.3.5.1 Bos taurus
-
 succinate dehydrogenase
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.5.1 using ammonium sulfate fractionation, solvent extraction and deoxycholate-ammonium sulfate extraction Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.3.5.1 heart
-
 Bos taurus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3.5.1 56
-
-
 Bos taurus

Storage Stability

EC Number Storage Stability Organism
1.3.5.1 -20°C, 1-2 weeks Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.5.1 additional information reduction of coenzyme Q and analogues, coenzyme Q2 is the most efficient electron acceptor, coenzyme Q10 in substrate quantities when supplemented with Triton X-100 and a lipid extract is about 75% as efficient as coenzyme Q2 Bos taurus ?
-
 ?
1.3.5.1 succinate + ubiquinone
-
 Bos taurus fumarate + ubiquinol
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.5.1 cytochrome b
-
 Bos taurus
1.3.5.1 FAD
-
 Bos taurus
1.3.5.1 additional information the enzyme contains 18-20% lipid by weight protein Bos taurus