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"integrated": "IPR004224",
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"name": {
"name": null,
"short": "QFR_TypeB_TM"
},
"description": [
{
"text": "<p>Quinol:fumarate reductase (QFR) Type B subfamily, transmembrane subunit; QFR couples the reduction of fumarate to succinate to the oxidation of quinol to quinone, the opposite reaction to that catalyzed by the related protein, succinate:quinone oxidoreductase (SQR). QFRs oxidize low potential quinols such as menaquinol and rhodoquinol and are involved in anaerobic respiration with fumarate as the terminal electron acceptor. SQR and QFR share a common subunit arrangement, composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Members of this subfamily are classified as Type B as they contain one transmembrane subunit and two heme groups. The heme and quinone binding sites reside in the transmembrane subunit. The structural arrangement allows efficient electron transfer between the catalytic subunit, through iron-sulfur centers, and the transmembrane subunit containing the electron donor (quinol). The Type B enzyme from Desulfovibrio gigas is capable of fumarate reduction and succinate oxidation. [[cite:PUB00007431], [cite:PUB00028408], [cite:PUB00080553], [cite:PUB00080554], [cite:PUB00080555], [cite:PUB00080556], [cite:PUB00080557], [cite:PUB00079621], [cite:PUB00015643], [cite:PUB00080558], [cite:PUB00079568], [cite:PUB00015715], [cite:PUB00015792]]</p>",
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"volume": "5",
"issue": "2",
"year": 2004,
"title": "Complex II from a structural perspective.",
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"raw_pages": "107-18",
"medline_journal": "Curr Protein Pept Sci",
"ISO_journal": "Curr. Protein Pept. Sci.",
"authors": [
"Horsefield R",
"Iwata S",
"Byrne B."
],
"DOI_URL": "http://dx.doi.org/10.2174/1389203043486847"
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"title": "Variation in proton donor/acceptor pathways in succinate:quinone oxidoreductases.",
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"raw_pages": "31-8",
"medline_journal": "FEBS Lett",
"ISO_journal": "FEBS Lett.",
"authors": [
"Cecchini G",
"Maklashina E",
"Yankovskaya V",
"Iverson TM",
"Iwata S."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0014-5793(03)00390-9"
},
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"PMID": 9492313,
"ISBN": null,
"volume": "251",
"issue": "1-2",
"year": 1998,
"title": "Deletion and site-directed mutagenesis of the Wolinella succinogenes fumarate reductase operon.",
"URL": null,
"raw_pages": "418-26",
"medline_journal": "Eur J Biochem",
"ISO_journal": "Eur. J. Biochem.",
"authors": [
"Simon J",
"Gross R",
"Ringel M",
"Schmidt E",
"Kroger A."
],
"DOI_URL": "http://dx.doi.org/10.1046/j.1432-1327.1998.2510418.x"
},
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"PMID": 11803024,
"ISBN": null,
"volume": "1553",
"issue": "1-2",
"year": 2002,
"title": "Quinol:fumarate oxidoreductases and succinate:quinone oxidoreductases: phylogenetic relationships, metal centres and membrane attachment.",
"URL": null,
"raw_pages": "158-70",
"medline_journal": "Biochim Biophys Acta",
"ISO_journal": "Biochim. Biophys. Acta",
"authors": [
"Lemos RS",
"Fernandes AS",
"Pereira MM",
"Gomes CM",
"Teixeira M."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0005-2728(01)00239-0"
},
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"volume": "1459",
"issue": "2-3",
"year": 2000,
"title": "Succinate: quinone oxidoreductases: new insights from X-ray crystal structures.",
"URL": null,
"raw_pages": "422-31",
"medline_journal": "Biochim Biophys Acta",
"ISO_journal": "Biochim. Biophys. Acta",
"authors": [
"Lancaster CR",
"Kroger A."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0005-2728(00)00180-8"
},
"PUB00079621": {
"PMID": 10981634,
"ISBN": null,
"volume": "10",
"issue": "4",
"year": 2000,
"title": "Analyzing your complexes: structure of the quinol-fumarate reductase respiratory complex.",
"URL": null,
"raw_pages": "448-55",
"medline_journal": "Curr Opin Struct Biol",
"ISO_journal": "Curr. Opin. Struct. Biol.",
"authors": [
"Iverson TM",
"Luna-Chavez C",
"Schroder I",
"Cecchini G",
"Rees DC."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0959-440X(00)00113-5"
},
"PUB00080556": {
"PMID": 11860177,
"ISBN": null,
"volume": "34",
"issue": "1",
"year": 2002,
"title": "The quinol:fumarate oxidoreductase from the sulphate reducing bacterium Desulfovibrio gigas: spectroscopic and redox studies.",
"URL": null,
"raw_pages": "21-30",
"medline_journal": "J Bioenerg Biomembr",
"ISO_journal": "J. Bioenerg. Biomembr.",
"authors": [
"Lemos RS",
"Gomes CM",
"LeGall J",
"Xavier AV",
"Teixeira M."
],
"DOI_URL": "http://dx.doi.org/10.1023/A:1013814619023"
},
"PUB00080554": {
"PMID": 11803015,
"ISBN": null,
"volume": "1553",
"issue": "1-2",
"year": 2002,
"title": "Fumarate respiration of Wolinella succinogenes: enzymology, energetics and coupling mechanism.",
"URL": null,
"raw_pages": "23-38",
"medline_journal": "Biochim Biophys Acta",
"ISO_journal": "Biochim. Biophys. Acta",
"authors": [
"Kroger A",
"Biel S",
"Simon J",
"Gross R",
"Unden G",
"Lancaster CR."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0005-2728(01)00234-1"
},
"PUB00015792": {
"PMID": 9210286,
"ISBN": null,
"volume": "1320",
"issue": "2",
"year": 1997,
"title": "Succinate: quinone oxidoreductases. Variations on a conserved theme.",
"URL": null,
"raw_pages": "107-41",
"medline_journal": "Biochim Biophys Acta",
"ISO_journal": "Biochim. Biophys. Acta",
"authors": [
"Hagerhall C."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0005-2728(97)00019-4"
},
"PUB00007431": {
"PMID": 10586875,
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"volume": "402",
"issue": "6760",
"year": 1999,
"title": "Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution.",
"URL": null,
"raw_pages": "377-85",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Lancaster CR",
"Kroger A",
"Auer M",
"Michel H."
],
"DOI_URL": "http://dx.doi.org/10.1038/46483"
},
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"volume": "543",
"issue": "1-3",
"year": 2003,
"title": "Is a Q-cycle-like mechanism operative in dihaemic succinate:quinone and quinol:fumarate oxidoreductases?",
"URL": null,
"raw_pages": "1-4",
"medline_journal": "FEBS Lett",
"ISO_journal": "FEBS Lett.",
"authors": [
"Pereira MM",
"Teixeira M."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0014-5793(03)00422-8"
},
"PUB00080553": {
"PMID": 11803019,
"ISBN": null,
"volume": "1553",
"issue": "1-2",
"year": 2002,
"title": "Succinate:quinone oxidoreductases from epsilon-proteobacteria.",
"URL": null,
"raw_pages": "84-101",
"medline_journal": "Biochim Biophys Acta",
"ISO_journal": "Biochim. Biophys. Acta",
"authors": [
"Lancaster CR",
"Simon J."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0005-2728(01)00230-4"
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"PUB00028408": {
"PMID": 11248702,
"ISBN": null,
"volume": "268",
"issue": "6",
"year": 2001,
"title": "A third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reduction.",
"URL": null,
"raw_pages": "1820-7",
"medline_journal": "Eur J Biochem",
"ISO_journal": "Eur. J. Biochem.",
"authors": [
"Lancaster CR",
"Gross R",
"Simon J."
],
"DOI_URL": "http://dx.doi.org/10.1046/j.1432-1327.2001.02053.x"
}
},
"set_info": {
"accession": "cl00881",
"name": "SQR_QFR_TM"
},
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 493,
"pathways": 0,
"proteins": 493,
"proteomes": 248,
"sets": 1,
"structural_models": {
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"bfvd": 0
},
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"taxa": 529
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"is_llm": false,
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"representative_structure": {
"accession": "2bs2",
"name": "QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES"
}
}
}
