Enzymes
| UniProtKB help_outline | 1 proteins |
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Name help_outline
a ubiquinone
Identifier
CHEBI:16389
(CAS: 1339-63-5)
help_outline
Charge
0
Formula
C9H10O4(C5H8)n
Search links
Involved in 49 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:9565Polymer name: a ubiquinonePolymerization index help_outline nFormula C9H10O4(C5H8)nCharge (0)(0)nMol File for the polymer
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Namehelp_outline
reduced [electron-transfer flavoprotein]
Identifier
RHEA-COMP:10686
Reactive part
help_outline
- Name help_outline FADH2 Identifier CHEBI:58307 Charge -2 Formula C27H33N9O15P2 InChIKeyhelp_outline YPZRHBJKEMOYQH-UYBVJOGSSA-L SMILEShelp_outline Cc1cc2Nc3c([nH]c(=O)[nH]c3=O)N(C[C@H](O)[C@H](O)[C@H](O)COP([O-])(=O)OP([O-])(=O)OC[C@H]3O[C@H]([C@H](O)[C@@H]3O)n3cnc4c(N)ncnc34)c2cc1C 2D coordinates Mol file for the small molecule Search links Involved in 161 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 ubiquinol
Identifier
CHEBI:17976
(CAS: 56275-39-9)
help_outline
Charge
0
Formula
C9H12O4(C5H8)n
Search links
Involved in 55 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:9566Polymer name: a ubiquinolPolymerization index help_outline nFormula C9H12O4(C5H8)nCharge (0)(0)nMol File for the polymer
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- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
oxidized [electron-transfer flavoprotein]
Identifier
RHEA-COMP:10685
Reactive part
help_outline
- Name help_outline FAD Identifier CHEBI:57692 Charge -3 Formula C27H30N9O15P2 InChIKeyhelp_outline IMGVNJNCCGXBHD-UYBVJOGSSA-K SMILEShelp_outline Cc1cc2nc3c(nc(=O)[n-]c3=O)n(C[C@H](O)[C@H](O)[C@H](O)COP([O-])(=O)OP([O-])(=O)OC[C@H]3O[C@H]([C@H](O)[C@@H]3O)n3cnc4c(N)ncnc34)c2cc1C 2D coordinates Mol file for the small molecule Search links Involved in 170 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:24052 | RHEA:24053 | RHEA:24054 | RHEA:24055 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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| MetaCyc help_outline |
Publications
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A new iron-sulfur flavoprotein of the respiratory chain. A component of the fatty acid beta oxidation pathway.
Ruzicka F.J., Beinert H.
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Electron-transfer flavoprotein-ubiquinone oxidoreductase from pig liver: purification and molecular, redox, and catalytic properties.
Beckmann J.D., Frerman F.E.
Electron-transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO) was purified to homogeneity from pig liver submitochondrial particles. It is comparable in molecular weight and general properties to ETF-QO from beef heart [Ruzicka, F. J., & Beinert, H. (1977) J. Biol. Chem. 252, 8440-8445], and t ... >> More
Electron-transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO) was purified to homogeneity from pig liver submitochondrial particles. It is comparable in molecular weight and general properties to ETF-QO from beef heart [Ruzicka, F. J., & Beinert, H. (1977) J. Biol. Chem. 252, 8440-8445], and the electron spin resonance signals of the reduced iron-sulfur cluster are essentially identical. ETF-QO catalyzes the transfer of electrons from electron-transfer flavoprotein (ETF) to nitro blue tetrazolium, with a sluggish reaction turnover number of about 10-30 min-1. In contrast, the enzyme rapidly disproportionates ETF semiquinone, with a turnover number of 200 s-1. The reverse reaction, comproportionation of oxidized and hydroquinone ETF, provides an enzymatic assay for ETF-QO with picomolar sensitivity. Equilibrium spectrophotometric titrations show that ETF-QO accepts a maximum of two electrons from ETF and accepts three electron equivalents from dithionite or by photochemical reduction. All electrons from the enzymatically or chemically reduced protein can be transferred to 2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinone (PB), and this reaction is readily reversible. Reduction of ETF-QO by 2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzohydroquinone is pH dependent and indicates the enzyme to have a redox potential that decreases by 47 mV per pH unit. Therefore, ETF-QO binds one to two protons upon reduction. The EO' at pH 7.3 is 38 mV. The ability of ETF-QO to catalyze the equilibration of ETF redox states has been used to evaluate the equilibrium 2ETFsq + nH+ in equilibrium ETFox + ETFhq.(ABSTRACT TRUNCATED AT 250 WORDS) << Less