A Cytochrome b/c1 Complex with Ubiquinol–Cytochrome c2 Oxidoreductase Activity from Rhodopseudomonas sphaeroides GA
A cytochrome b/c1 complex which catalyses the reduction of cytochrome c by ubiquinol has been isolated from Rhodopseudomonas sphaeroides GA. It contains two hemes b and substoichiometric amounts of ubiquinone‐10 and of the Rieske Fe‐S center per cytochrome c1, and is essentially free of reaction cen...
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| Veröffentlicht in: | European journal of biochemistry 1982-08, Vol.126 (1), p.105-111 |
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| container_title | European journal of biochemistry |
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| creator | GABELLINI, Nadia BOWYER, John R. HURT, Eduard MELANDRI, B. Andrea HAUSKA, Günter |
| description | A cytochrome b/c1 complex which catalyses the reduction of cytochrome c by ubiquinol has been isolated from Rhodopseudomonas sphaeroides GA. It contains two hemes b and substoichiometric amounts of ubiquinone‐10 and of the Rieske Fe‐S center per cytochrome c1, and is essentially free of reaction center and bacteriochlorophyll. The complex consists of three major polypeptides with apparent molecular masses of 40, 34 and 25 kDa. The 34‐kDa polypeptide carries heme. Cytochrome c1 has a midpoint potential of 285 mV. For cytochrome b two midpoint potentials, at 50 and –60 mV, at pH 7.4, can be derived if one assumes two components of equal amount. Ubiquinol–cytochrome c oxidoreductase activity is specific for ubiquinol and bacterial cytochromes c, and is inhibited by antimycin A and 5‐n‐undecyl‐6‐hydroxy‐4,7‐dioxobenzothiazole. The complex shows oxidant‐induced reduction of cytochrome b. |
| doi_str_mv | 10.1111/j.1432-1033.1982.tb06753.x |
| format | Article |
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Andrea ; HAUSKA, Günter</creator><creatorcontrib>GABELLINI, Nadia ; BOWYER, John R. ; HURT, Eduard ; MELANDRI, B. Andrea ; HAUSKA, Günter</creatorcontrib><description>A cytochrome b/c1 complex which catalyses the reduction of cytochrome c by ubiquinol has been isolated from Rhodopseudomonas sphaeroides GA. It contains two hemes b and substoichiometric amounts of ubiquinone‐10 and of the Rieske Fe‐S center per cytochrome c1, and is essentially free of reaction center and bacteriochlorophyll. The complex consists of three major polypeptides with apparent molecular masses of 40, 34 and 25 kDa. The 34‐kDa polypeptide carries heme. Cytochrome c1 has a midpoint potential of 285 mV. For cytochrome b two midpoint potentials, at 50 and –60 mV, at pH 7.4, can be derived if one assumes two components of equal amount. Ubiquinol–cytochrome c oxidoreductase activity is specific for ubiquinol and bacterial cytochromes c, and is inhibited by antimycin A and 5‐n‐undecyl‐6‐hydroxy‐4,7‐dioxobenzothiazole. The complex shows oxidant‐induced reduction of cytochrome b.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1982.tb06753.x</identifier><identifier>PMID: 6290210</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Chemical Phenomena ; Chemistry ; Electron Spin Resonance Spectroscopy ; Electron Transport Complex III ; Multienzyme Complexes - isolation & purification ; Multienzyme Complexes - metabolism ; NADH, NADPH Oxidoreductases - isolation & purification ; Oxidation-Reduction ; Quinone Reductases - isolation & purification ; Quinone Reductases - metabolism ; Rhodobacter sphaeroides - enzymology</subject><ispartof>European journal of biochemistry, 1982-08, Vol.126 (1), p.105-111</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6290210$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>GABELLINI, Nadia</creatorcontrib><creatorcontrib>BOWYER, John R.</creatorcontrib><creatorcontrib>HURT, Eduard</creatorcontrib><creatorcontrib>MELANDRI, B. Andrea</creatorcontrib><creatorcontrib>HAUSKA, Günter</creatorcontrib><title>A Cytochrome b/c1 Complex with Ubiquinol–Cytochrome c2 Oxidoreductase Activity from Rhodopseudomonas sphaeroides GA</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>A cytochrome b/c1 complex which catalyses the reduction of cytochrome c by ubiquinol has been isolated from Rhodopseudomonas sphaeroides GA. It contains two hemes b and substoichiometric amounts of ubiquinone‐10 and of the Rieske Fe‐S center per cytochrome c1, and is essentially free of reaction center and bacteriochlorophyll. The complex consists of three major polypeptides with apparent molecular masses of 40, 34 and 25 kDa. The 34‐kDa polypeptide carries heme. Cytochrome c1 has a midpoint potential of 285 mV. For cytochrome b two midpoint potentials, at 50 and –60 mV, at pH 7.4, can be derived if one assumes two components of equal amount. Ubiquinol–cytochrome c oxidoreductase activity is specific for ubiquinol and bacterial cytochromes c, and is inhibited by antimycin A and 5‐n‐undecyl‐6‐hydroxy‐4,7‐dioxobenzothiazole. The complex shows oxidant‐induced reduction of cytochrome b.</description><subject>Chemical Phenomena</subject><subject>Chemistry</subject><subject>Electron Spin Resonance Spectroscopy</subject><subject>Electron Transport Complex III</subject><subject>Multienzyme Complexes - isolation & purification</subject><subject>Multienzyme Complexes - metabolism</subject><subject>NADH, NADPH Oxidoreductases - isolation & purification</subject><subject>Oxidation-Reduction</subject><subject>Quinone Reductases - isolation & purification</subject><subject>Quinone Reductases - metabolism</subject><subject>Rhodobacter sphaeroides - enzymology</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkV1LwzAUhoMoOqc_QQheeNfu5KNteiVzOBWEgR_XIWlSltEutWl1u_M_-A_9JXY4xNycwPNw4LwvQpcEYjK8ySomnNGIAGMxyQWNOw1plrB4c4BGf-gQjQAIj2iepCfoNIQVAKR5mh2j45TmQAmMUD_Fs23ni2Xra4v1pCB45uumshv84bolftXurXdrX31_fv0TC4oXG2d8a01fdCpYPC069-66LS4HAT8tvfFNsL3xtV-rgEOzVLb1ztiA76Zn6KhUVbDn-zlGr_Pbl9l99Li4e5hNH6OGEZ5ElhmSQW5AEWpUmpWpUMMfiqwUIitEyfNSE6GNEEJrM9wEUAqWa654CXnKxujqd2_T-rfehk7WLhS2qtTa-j7IjNOEc8oH8WIv9rq2Rjatq1W7lfucBn79yz9cZbd_mIDcFSJXcpe63KUud4XIfSFyI-e3N88EEvYDD66B6Q</recordid><startdate>198208</startdate><enddate>198208</enddate><creator>GABELLINI, Nadia</creator><creator>BOWYER, John R.</creator><creator>HURT, Eduard</creator><creator>MELANDRI, B. Andrea</creator><creator>HAUSKA, Günter</creator><general>Blackwell Publishing Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>198208</creationdate><title>A Cytochrome b/c1 Complex with Ubiquinol–Cytochrome c2 Oxidoreductase Activity from Rhodopseudomonas sphaeroides GA</title><author>GABELLINI, Nadia ; BOWYER, John R. ; HURT, Eduard ; MELANDRI, B. Andrea ; HAUSKA, Günter</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p3145-e3d1709d0a12da67f68a0a10c7f887c8f49fb18bd888bbd29000f839b4a4f0963</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>Chemical Phenomena</topic><topic>Chemistry</topic><topic>Electron Spin Resonance Spectroscopy</topic><topic>Electron Transport Complex III</topic><topic>Multienzyme Complexes - isolation & purification</topic><topic>Multienzyme Complexes - metabolism</topic><topic>NADH, NADPH Oxidoreductases - isolation & purification</topic><topic>Oxidation-Reduction</topic><topic>Quinone Reductases - isolation & purification</topic><topic>Quinone Reductases - metabolism</topic><topic>Rhodobacter sphaeroides - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>GABELLINI, Nadia</creatorcontrib><creatorcontrib>BOWYER, John R.</creatorcontrib><creatorcontrib>HURT, Eduard</creatorcontrib><creatorcontrib>MELANDRI, B. Andrea</creatorcontrib><creatorcontrib>HAUSKA, Günter</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>GABELLINI, Nadia</au><au>BOWYER, John R.</au><au>HURT, Eduard</au><au>MELANDRI, B. Andrea</au><au>HAUSKA, Günter</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Cytochrome b/c1 Complex with Ubiquinol–Cytochrome c2 Oxidoreductase Activity from Rhodopseudomonas sphaeroides GA</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1982-08</date><risdate>1982</risdate><volume>126</volume><issue>1</issue><spage>105</spage><epage>111</epage><pages>105-111</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>A cytochrome b/c1 complex which catalyses the reduction of cytochrome c by ubiquinol has been isolated from Rhodopseudomonas sphaeroides GA. It contains two hemes b and substoichiometric amounts of ubiquinone‐10 and of the Rieske Fe‐S center per cytochrome c1, and is essentially free of reaction center and bacteriochlorophyll. The complex consists of three major polypeptides with apparent molecular masses of 40, 34 and 25 kDa. The 34‐kDa polypeptide carries heme. Cytochrome c1 has a midpoint potential of 285 mV. For cytochrome b two midpoint potentials, at 50 and –60 mV, at pH 7.4, can be derived if one assumes two components of equal amount. Ubiquinol–cytochrome c oxidoreductase activity is specific for ubiquinol and bacterial cytochromes c, and is inhibited by antimycin A and 5‐n‐undecyl‐6‐hydroxy‐4,7‐dioxobenzothiazole. The complex shows oxidant‐induced reduction of cytochrome b.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>6290210</pmid><doi>10.1111/j.1432-1033.1982.tb06753.x</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-2956 |
| ispartof | European journal of biochemistry, 1982-08, Vol.126 (1), p.105-111 |
| issn | 0014-2956 1432-1033 |
| language | eng |
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| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Chemical Phenomena Chemistry Electron Spin Resonance Spectroscopy Electron Transport Complex III Multienzyme Complexes - isolation & purification Multienzyme Complexes - metabolism NADH, NADPH Oxidoreductases - isolation & purification Oxidation-Reduction Quinone Reductases - isolation & purification Quinone Reductases - metabolism Rhodobacter sphaeroides - enzymology |
| title | A Cytochrome b/c1 Complex with Ubiquinol–Cytochrome c2 Oxidoreductase Activity from Rhodopseudomonas sphaeroides GA |
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