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Literature summary extracted from

  • Shimizu, H.; Osanai, A.; Sakamoto, K.; Inaoka, D.K.; Shiba, T.; Harada, S.; Kita, K.
    Crystal structure of mitochondrial quinol-fumarate reductase from the parasitic nematode Ascaris suum (2012), J. Biochem., 151, 589-592.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.5.1 purified native enzyme by dialysis method using a reservoir solution containing 15% w/v PEG 3350, 100 mM Tris-HCl, pH 8.4, 200 mM NaCl, 1 mM sodium malonate or fumarate, 0.06% w/v n-dodecyl ethylene glycol monoether C12E8, and 0.04% w/v n-dodecyl-bet-D-maltoside, 2-3 days, X-ray diffraction structure determination and analysis at 2.81-2.91 A resolution, molecular replacement Ascaris suum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.5.1 mitochondrion
-
 Ascaris suum 5739
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.3.5.1 Fe2+ of the three iron-sulfur centres bound to subunit Ip, [2Fe-2S] is coordinated by four cysteine residues,B89, B94, B97 and B109, and located in the N-terminal domain, whereas [4Fe-4S] and [3Fe-4S] that are coordinated by four, B182, B185, B188, and B249, and three, B192, B239 and B245, cysteine residues, respectively, are bound to the C-terminal domain. These iron-sulfur centres are also surrounded with highly conserved hydrophobic amino acid residues Ascaris suum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.5.1 succinate + rhodoquinone Ascaris suum
-
 fumarate + rhodoquinol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.5.1 Ascaris suum P92507
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.5.1 native enzyme from muscle mitochondria by anion exchange chromatography Ascaris suum

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.3.5.1 muscle
-
 Ascaris suum
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.5.1 succinate + rhodoquinone
-
 Ascaris suum fumarate + rhodoquinol
-
 ?
1.3.5.1 succinate + rhodoquinone rhodoquinone binding site, overview Ascaris suum fumarate + rhodoquinol
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.5.1 More the enzyme structure comprises four subunits and five co-factors, subunit structure comparisons, overview Ascaris suum
1.3.5.1 tetramer QFR is composed of Fp, Ip, CybL and CybS subunits Ascaris suum

Synonyms

EC Number Synonyms Comment Organism
1.3.5.1 QFR
-
 Ascaris suum
1.3.5.1 quinol-fumarate reductase
-
 Ascaris suum

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.5.1 FAD the FAD prosthetic group is held in the FAD binding domain by a covalent bond to His A79 and by hydrogen bonds with highly conserved residues, overview Ascaris suum
1.3.5.1 heme
-
 Ascaris suum
1.3.5.1 additional information the enzyme structure comprises four subunits and five co-factors, cofactor structure comparisons, overview Ascaris suum

General Information

EC Number General Information Comment Organism
1.3.5.1 additional information enzyme structure-function relationship, overview Ascaris suum
1.3.5.1 physiological function the enzyme is part of the complex II, which in the anaerobic respiratory chain of the parasitic nematode Ascaris suum, couples the reduction of fumarate to the oxidation of rhodoquinol. Critical role of the low redox potential of rhodoquinol in the fumarate reduction of Ascaris suum complex II Ascaris suum