Literature summary for 1.3.5.1 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.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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

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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
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)

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

Organism

Organism	UniProt	Comment	Textmining
Ascaris suum	P92507	-	-

Purification (Commentary)

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

Source Tissue

Source Tissue	Comment	Organism	Textmining
muscle	-	Ascaris suum	-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms	Comment	Organism
QFR	-	Ascaris suum
quinol-fumarate reductase	-	Ascaris suum

Cofactor

Cofactor	Comment	Organism	Structure
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
heme	-	Ascaris suum
additional information	the enzyme structure comprises four subunits and five co-factors, cofactor structure comparisons, overview	Ascaris suum

General Information

General Information	Comment	Organism
additional information	enzyme structure-function relationship, overview	Ascaris suum
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

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Release 2023.1 (January 2023)