Enzymes
| UniProtKB help_outline | 6,008 proteins |
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Reaction participants Show >> << Hide
- Name help_outline CoA Identifier CHEBI:57287 (Beilstein: 11604429) help_outline Charge -4 Formula C21H32N7O16P3S InChIKeyhelp_outline RGJOEKWQDUBAIZ-IBOSZNHHSA-J SMILEShelp_outline CC(C)(COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12)[C@@H](O)C(=O)NCCC(=O)NCCS 2D coordinates Mol file for the small molecule Search links Involved in 1,500 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
oxidized [2Fe-2S]-[ferredoxin]
Identifier
RHEA-COMP:10000
Reactive part
help_outline
- Name help_outline [2Fe-2S]2+ Identifier CHEBI:33737 Charge 2 Formula Fe2S2 InChIKeyhelp_outline XSOVBBGAMBLACL-UHFFFAOYSA-N SMILEShelp_outline S1[Fe+]S[Fe+]1 2D coordinates Mol file for the small molecule Search links Involved in 238 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline pyruvate Identifier CHEBI:15361 (Beilstein: 3587721; CAS: 57-60-3) help_outline Charge -1 Formula C3H3O3 InChIKeyhelp_outline LCTONWCANYUPML-UHFFFAOYSA-M SMILEShelp_outline CC(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 215 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline acetyl-CoA Identifier CHEBI:57288 (Beilstein: 8468140) help_outline Charge -4 Formula C23H34N7O17P3S InChIKeyhelp_outline ZSLZBFCDCINBPY-ZSJPKINUSA-J SMILEShelp_outline CC(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 352 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CO2 Identifier CHEBI:16526 (Beilstein: 1900390; CAS: 124-38-9) help_outline Charge 0 Formula CO2 InChIKeyhelp_outline CURLTUGMZLYLDI-UHFFFAOYSA-N SMILEShelp_outline O=C=O 2D coordinates Mol file for the small molecule Search links Involved in 997 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- 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
reduced [2Fe-2S]-[ferredoxin]
Identifier
RHEA-COMP:10001
Reactive part
help_outline
- Name help_outline [2Fe-2S]1+ Identifier CHEBI:33738 Charge 1 Formula Fe2S2 InChIKeyhelp_outline MAGIRAZQQVQNKP-UHFFFAOYSA-N SMILEShelp_outline S1[Fe]S[Fe+]1 2D coordinates Mol file for the small molecule Search links Involved in 238 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:12765 | RHEA:12766 | RHEA:12767 | RHEA:12768 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Structure and electron transfer mechanism of pyruvate:ferredoxin oxidoreductase.
Charon M.H., Volbeda A., Chabriere E., Pieulle L., Fontecilla-Camps J.C.
The first crystal structure of pyruvate:ferredoxin oxidoreductase to be determined has provided significant new information on its structural organization and redox chemistry. Spectroscopic analyses of a radical reaction intermediate have shed more light on its thiamin-based mechanism of catalysis ... >> More
The first crystal structure of pyruvate:ferredoxin oxidoreductase to be determined has provided significant new information on its structural organization and redox chemistry. Spectroscopic analyses of a radical reaction intermediate have shed more light on its thiamin-based mechanism of catalysis. Different approaches have been used to study the interaction between the enzyme and ferredoxin, its redox partner. << Less
Curr Opin Struct Biol 9:663-669(1999) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Isolation and characterization of the pyruvate-ferredoxin oxidoreductase from the sulfate-reducing bacterium Desulfovibrio africanus.
Pieulle L., Guigliarelli B., Asso M., Dole F., Bernadac A., Hatchikian E.C.
We report the first purification and characterization of a pyruvate-ferredoxin oxidoreductase (POR) from a sulfate-reducing bacterium, Desulfovibrio africanus. The enzyme as isolated is highly stable in the presence of oxygen and exhibits a specific activity of 14 U/mg. D. africanus POR is a 256 k ... >> More
We report the first purification and characterization of a pyruvate-ferredoxin oxidoreductase (POR) from a sulfate-reducing bacterium, Desulfovibrio africanus. The enzyme as isolated is highly stable in the presence of oxygen and exhibits a specific activity of 14 U/mg. D. africanus POR is a 256 kDa homodimer which contains thiamine pyrophosphate (TPP) and iron-sulfur clusters. EPR spectroscopic study of the enzyme indicates the presence of three [4Fe-4S]2+/1-centers/subunits. The midpoint potentials of the three centers are -390 mV, -515 mV and -540 mV. The catalytic mechanism of POR involves a free radical intermediate which disappears when coenzyme A is added. This behaviour is discussed in terms of an electron-transport chain from TPP to the acceptor. The enzyme activated by dithioerythritol shows an exceptionally high activity compared with other mesophile PORs and becomes very sensitive to oxygen in contrast to the enzyme before activation. The comparison of EPR spectra given by the as isolated and activated enzymes shows that neither the nature, nor the arrangement of FeS centers are affected by the activation process. D. africanus ferredoxins I and II are involved as the physiological electron carriers of the enzyme. POR was shown to be located in the cytoplasm by immunogold labelling. << Less
Biochim. Biophys. Acta 1250:49-59(1995) [PubMed] [EuropePMC]
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Pyruvate-ferredoxin oxidoreductase. IV. Studies on the reaction mechanism.
Uyeda K., Rabinowitz J.C.
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Photoreduction of ferredoxin and its use in carbon dioxide fixation by a subcellular system from a photosynthetic bacterium.
Evans M.C., Buchanan B.B.
Proc Natl Acad Sci U S A 53:1420-1425(1965) [PubMed] [EuropePMC]