Enzymes
UniProtKB help_outline | 2 proteins |
Reaction participants Show >> << Hide
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Name help_outline
a rhodoquinone
Identifier
CHEBI:194432
Charge
0
Formula
(C5H8)n.C8H9NO3
Search links
Involved in 1 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:18569Polymer name: a rhodoquinonePolymerization index help_outline nFormula C8H9NO3(C5H8)nCharge (0)(0)nMol File for the polymer
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- Name help_outline succinate Identifier CHEBI:30031 (Beilstein: 1863859; CAS: 56-14-4) help_outline Charge -2 Formula C4H4O4 InChIKeyhelp_outline KDYFGRWQOYBRFD-UHFFFAOYSA-L SMILEShelp_outline [O-]C(=O)CCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 331 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Name help_outline
a rhodoquinol
Identifier
CHEBI:194433
Charge
0
Formula
(C5H8)n.C8H11NO3
Search links
Involved in 1 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:18570Polymer name: a rhodoquinolPolymerization index help_outline nFormula C8H11NO3(C5H8)nCharge (0)(0)nMol File for the polymer
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- Name help_outline fumarate Identifier CHEBI:29806 (Beilstein: 1861276; CAS: 142-42-7) help_outline Charge -2 Formula C4H2O4 InChIKeyhelp_outline VZCYOOQTPOCHFL-OWOJBTEDSA-L SMILEShelp_outline [O-]C(=O)\C=C\C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 40 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:75711 | RHEA:75712 | RHEA:75713 | RHEA:75714 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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EC numbers help_outline | ||||
MetaCyc help_outline |
Related reactions help_outline
More general form(s) of this reaction
Publications
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Role of complex II in anaerobic respiration of the parasite mitochondria from Ascaris suum and Plasmodium falciparum.
Kita K., Hirawake H., Miyadera H., Amino H., Takeo S.
Parasites have developed a variety of physiological functions necessary for existence within the specialized environment of the host. Regarding energy metabolism, which is an essential factor for survival, parasites adapt to low oxygen tension in host mammals using metabolic systems that are very ... >> More
Parasites have developed a variety of physiological functions necessary for existence within the specialized environment of the host. Regarding energy metabolism, which is an essential factor for survival, parasites adapt to low oxygen tension in host mammals using metabolic systems that are very different from that of the host. The majority of parasites do not use the oxygen available within the host, but employ systems other than oxidative phosphorylation for ATP synthesis. In addition, all parasites have a life cycle. In many cases, the parasite employs aerobic metabolism during their free-living stage outside the host. In such systems, parasite mitochondria play diverse roles. In particular, marked changes in the morphology and components of the mitochondria during the life cycle are very interesting elements of biological processes such as developmental control and environmental adaptation. Recent research has shown that the mitochondrial complex II plays an important role in the anaerobic energy metabolism of parasites inhabiting hosts, by acting as quinol-fumarate reductase. << Less
Biochim. Biophys. Acta 1553:123-139(2002) [PubMed] [EuropePMC]
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Electron-transfer complexes of Ascaris suum muscle mitochondria. III. Composition and fumarate reductase activity of complex II.
Kita K., Takamiya S., Furushima R., Ma Y.C., Suzuki H., Ozawa T., Oya H.
Complex II of the anaerobic respiratory chain in Ascaris muscle mitochondria showed a high fumarate reductase activity when reduced methyl viologen was used as the electron donor. The maximum activity was 49 mumol/min per mg protein, which is much higher than that of the mammalian counterpart. The ... >> More
Complex II of the anaerobic respiratory chain in Ascaris muscle mitochondria showed a high fumarate reductase activity when reduced methyl viologen was used as the electron donor. The maximum activity was 49 mumol/min per mg protein, which is much higher than that of the mammalian counterpart. The mitochondria of Ascaris-fertilized eggs, which require oxygen for its development, also showed fumarate reductase activity with a specific activity intermediate between those of adult Ascaris and mammals. Antibody against the Ascaris flavoprotein subunit reacted with the mammalian counterparts, whereas those against the Ascaris iron-sulfur protein subunit did not crossreact, although the amino acid compositions of the subunits in Ascaris and bovine heart were quite similar. Cytochrome b-558 of Ascaris complex II was separated from flavoprotein and iron-sulphur protein subunits by high performance liquid chromatography with a gel permeation system in the presence of Sarkosyl. Isolated cytochrome b-558 is composed of two hydrophobic polypeptides with molecular masses of 17.2 and 12.5 kDa determined by gradient gel, which correspond to the two small subunits of complex II. Amino acid compositions of these small subunits showed little similarity with those of cytochrome b-560 of bovine heart complex II. NADH-fumarate reductase, which is the final enzyme complex in the anaerobic respiratory chain in Ascaris, was reconstituted with bovine heart complex I, Ascaris complex II and phospholipids. The maximum activity was 430 nmol/min per mg protein of complex II. Rhodoquinone was essential for this reconstitution, whereas ubiquinone showed no effect. The results clearly indicate the unique role of Ascaris complex II as fumarate reductase and the indispensability of rhodoquinone as the low-potential electron carrier in the NADH-fumarate reductase system. << Less
Biochim. Biophys. Acta 935:130-140(1988) [PubMed] [EuropePMC]