The antioxidant functions of cytochrome c
Low (C 1/2=1.5×10 −7 M) concentrations of horse cytochrome c strongly inhibit H 2O 2 production by rat heart mitochondria under conditions of reverse electron transfer from succinate to NAD +. The effect is abolished by binding of cytochrome c with liposomes and is not prevented by SOD. Yeast cytoch...
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| Veröffentlicht in: | FEBS letters 1999-11, Vol.462 (1), p.192-198 |
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| creator | Korshunov, Sergey S Krasnikov, Boris F Pereverzev, Mikhail O Skulachev, Vladimir P |
| description | Low (C
1/2=1.5×10
−7 M) concentrations of horse cytochrome
c strongly inhibit H
2O
2 production by rat heart mitochondria under conditions of reverse electron transfer from succinate to NAD
+. The effect is abolished by binding of cytochrome
c with liposomes and is not prevented by SOD. Yeast cytochrome
c is much less effective than the horse protein whereas acetylated horse cytochrome
c is without effect. H
2O
2 formation stimulated by antimycin A is resistant to added cytochrome
c. In inside-out submitochondrial vesicles, H
2O
2 production is suppressed by all three cytochrome
c samples tested, but at higher concentrations (C
1/2 is about 5×10
−7 M). In vesicles, SOD abolishes the cytochrome
c inhibition. We conclude that extramitochondrial cytochrome
c is competent in down-regulation of the Complex I H
2O
2 production linked to the reverse electron transfer. Such an effect is absent in the inside-out submitochondrial vesicles where another antioxidant cytochrome
c function can be observed, i.e. the oxidation of O
2
−
to O
2. A possible role of cytochrome
c in the antioxidant defence is discussed. |
| doi_str_mv | 10.1016/S0014-5793(99)01525-2 |
| format | Article |
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1/2=1.5×10
−7 M) concentrations of horse cytochrome
c strongly inhibit H
2O
2 production by rat heart mitochondria under conditions of reverse electron transfer from succinate to NAD
+. The effect is abolished by binding of cytochrome
c with liposomes and is not prevented by SOD. Yeast cytochrome
c is much less effective than the horse protein whereas acetylated horse cytochrome
c is without effect. H
2O
2 formation stimulated by antimycin A is resistant to added cytochrome
c. In inside-out submitochondrial vesicles, H
2O
2 production is suppressed by all three cytochrome
c samples tested, but at higher concentrations (C
1/2 is about 5×10
−7 M). In vesicles, SOD abolishes the cytochrome
c inhibition. We conclude that extramitochondrial cytochrome
c is competent in down-regulation of the Complex I H
2O
2 production linked to the reverse electron transfer. Such an effect is absent in the inside-out submitochondrial vesicles where another antioxidant cytochrome
c function can be observed, i.e. the oxidation of O
2
−
to O
2. A possible role of cytochrome
c in the antioxidant defence is discussed.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(99)01525-2</identifier><identifier>PMID: 10580118</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Animals ; Anti-Bacterial Agents - pharmacology ; Antimycin A - pharmacology ; Antioxidant ; Antioxidants - metabolism ; Cattle ; Cytochrome c ; Cytochrome c Group - metabolism ; DNP, 2,4-p-dinitrophenol ; FCCP, p-trifluoromethylcarbonylcyanide phenylhydrazone ; Hydrogen Peroxide - metabolism ; In Vitro Techniques ; Liposomes ; Mitochondria, Heart - drug effects ; Mitochondria, Heart - metabolism ; Mitochondrion ; PTP, permeability transition pore ; Rats ; Reactive oxygen species ; Reactive Oxygen Species - metabolism ; ROS, reactive oxygen species ; SOD, superoxide dismutase ; Superoxide oxidation ; TPP+, tetraphenyl phosphonium</subject><ispartof>FEBS letters, 1999-11, Vol.462 (1), p.192-198</ispartof><rights>1999 Federation of European Biochemical Societies</rights><rights>FEBS Letters 462 (1999) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4732-6590fbf80cdf2d94387ca53ef7ee08170c17c9411496490bd4b4e51a3744a0473</citedby><cites>FETCH-LOGICAL-c4732-6590fbf80cdf2d94387ca53ef7ee08170c17c9411496490bd4b4e51a3744a0473</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2899%2901525-2$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579399015252$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3536,27903,27904,45553,45554,46387,46811,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10580118$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Korshunov, Sergey S</creatorcontrib><creatorcontrib>Krasnikov, Boris F</creatorcontrib><creatorcontrib>Pereverzev, Mikhail O</creatorcontrib><creatorcontrib>Skulachev, Vladimir P</creatorcontrib><title>The antioxidant functions of cytochrome c</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Low (C
1/2=1.5×10
−7 M) concentrations of horse cytochrome
c strongly inhibit H
2O
2 production by rat heart mitochondria under conditions of reverse electron transfer from succinate to NAD
+. The effect is abolished by binding of cytochrome
c with liposomes and is not prevented by SOD. Yeast cytochrome
c is much less effective than the horse protein whereas acetylated horse cytochrome
c is without effect. H
2O
2 formation stimulated by antimycin A is resistant to added cytochrome
c. In inside-out submitochondrial vesicles, H
2O
2 production is suppressed by all three cytochrome
c samples tested, but at higher concentrations (C
1/2 is about 5×10
−7 M). In vesicles, SOD abolishes the cytochrome
c inhibition. We conclude that extramitochondrial cytochrome
c is competent in down-regulation of the Complex I H
2O
2 production linked to the reverse electron transfer. Such an effect is absent in the inside-out submitochondrial vesicles where another antioxidant cytochrome
c function can be observed, i.e. the oxidation of O
2
−
to O
2. A possible role of cytochrome
c in the antioxidant defence is discussed.</description><subject>Animals</subject><subject>Anti-Bacterial Agents - pharmacology</subject><subject>Antimycin A - pharmacology</subject><subject>Antioxidant</subject><subject>Antioxidants - metabolism</subject><subject>Cattle</subject><subject>Cytochrome c</subject><subject>Cytochrome c Group - metabolism</subject><subject>DNP, 2,4-p-dinitrophenol</subject><subject>FCCP, p-trifluoromethylcarbonylcyanide phenylhydrazone</subject><subject>Hydrogen Peroxide - metabolism</subject><subject>In Vitro Techniques</subject><subject>Liposomes</subject><subject>Mitochondria, Heart - drug effects</subject><subject>Mitochondria, Heart - metabolism</subject><subject>Mitochondrion</subject><subject>PTP, permeability transition pore</subject><subject>Rats</subject><subject>Reactive oxygen species</subject><subject>Reactive Oxygen Species - metabolism</subject><subject>ROS, reactive oxygen species</subject><subject>SOD, superoxide dismutase</subject><subject>Superoxide oxidation</subject><subject>TPP+, tetraphenyl phosphonium</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkMtOwzAQRS0EouXxCaCsEF0EbMeO7RWCqqVIlVhQ1lbijFWjPErcAP178qgQO1iNxnPmjnUQuiD4hmAS375gTFjIhYqulZpgwikP6QEaEymiMGKxPETjH2SETrx_w20viTpGI4K5xITIMZqs1hAk5dZVXy5ra2Cb0rRd6YPKBma3rcy6rgoIzBk6sknu4XxfT9HrfLaaLsLl8-PT9H4ZGiYiGsZcYZtaiU1maaZYJIVJeARWAGBJBDZEGMUIYSpmCqcZSxlwkkSCsQS3Eafoasjd1NV7A36rC-cN5HlSQtV4HauIUiloC_IBNHXlfQ1Wb2pXJPVOE6w7R7p3pDsBWindO9Ld3uX-QJMWkP3aGqS0wGIAPl0Ou_-l6vnsgfaTbqBU_9zduhuioDX24aDW3jgoDWSuBrPVWeX--O030O6IFg</recordid><startdate>19991126</startdate><enddate>19991126</enddate><creator>Korshunov, Sergey S</creator><creator>Krasnikov, Boris F</creator><creator>Pereverzev, Mikhail O</creator><creator>Skulachev, Vladimir P</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19991126</creationdate><title>The antioxidant functions of cytochrome c</title><author>Korshunov, Sergey S ; Krasnikov, Boris F ; Pereverzev, Mikhail O ; Skulachev, Vladimir P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4732-6590fbf80cdf2d94387ca53ef7ee08170c17c9411496490bd4b4e51a3744a0473</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Animals</topic><topic>Anti-Bacterial Agents - pharmacology</topic><topic>Antimycin A - pharmacology</topic><topic>Antioxidant</topic><topic>Antioxidants - metabolism</topic><topic>Cattle</topic><topic>Cytochrome c</topic><topic>Cytochrome c Group - metabolism</topic><topic>DNP, 2,4-p-dinitrophenol</topic><topic>FCCP, p-trifluoromethylcarbonylcyanide phenylhydrazone</topic><topic>Hydrogen Peroxide - metabolism</topic><topic>In Vitro Techniques</topic><topic>Liposomes</topic><topic>Mitochondria, Heart - drug effects</topic><topic>Mitochondria, Heart - metabolism</topic><topic>Mitochondrion</topic><topic>PTP, permeability transition pore</topic><topic>Rats</topic><topic>Reactive oxygen species</topic><topic>Reactive Oxygen Species - metabolism</topic><topic>ROS, reactive oxygen species</topic><topic>SOD, superoxide dismutase</topic><topic>Superoxide oxidation</topic><topic>TPP+, tetraphenyl phosphonium</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Korshunov, Sergey S</creatorcontrib><creatorcontrib>Krasnikov, Boris F</creatorcontrib><creatorcontrib>Pereverzev, Mikhail O</creatorcontrib><creatorcontrib>Skulachev, Vladimir P</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Korshunov, Sergey S</au><au>Krasnikov, Boris F</au><au>Pereverzev, Mikhail O</au><au>Skulachev, Vladimir P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The antioxidant functions of cytochrome c</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1999-11-26</date><risdate>1999</risdate><volume>462</volume><issue>1</issue><spage>192</spage><epage>198</epage><pages>192-198</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Low (C
1/2=1.5×10
−7 M) concentrations of horse cytochrome
c strongly inhibit H
2O
2 production by rat heart mitochondria under conditions of reverse electron transfer from succinate to NAD
+. The effect is abolished by binding of cytochrome
c with liposomes and is not prevented by SOD. Yeast cytochrome
c is much less effective than the horse protein whereas acetylated horse cytochrome
c is without effect. H
2O
2 formation stimulated by antimycin A is resistant to added cytochrome
c. In inside-out submitochondrial vesicles, H
2O
2 production is suppressed by all three cytochrome
c samples tested, but at higher concentrations (C
1/2 is about 5×10
−7 M). In vesicles, SOD abolishes the cytochrome
c inhibition. We conclude that extramitochondrial cytochrome
c is competent in down-regulation of the Complex I H
2O
2 production linked to the reverse electron transfer. Such an effect is absent in the inside-out submitochondrial vesicles where another antioxidant cytochrome
c function can be observed, i.e. the oxidation of O
2
−
to O
2. A possible role of cytochrome
c in the antioxidant defence is discussed.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>10580118</pmid><doi>10.1016/S0014-5793(99)01525-2</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | FEBS letters, 1999-11, Vol.462 (1), p.192-198 |
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| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Wiley Free Content; Alma/SFX Local Collection |
| subjects | Animals Anti-Bacterial Agents - pharmacology Antimycin A - pharmacology Antioxidant Antioxidants - metabolism Cattle Cytochrome c Cytochrome c Group - metabolism DNP, 2,4-p-dinitrophenol FCCP, p-trifluoromethylcarbonylcyanide phenylhydrazone Hydrogen Peroxide - metabolism In Vitro Techniques Liposomes Mitochondria, Heart - drug effects Mitochondria, Heart - metabolism Mitochondrion PTP, permeability transition pore Rats Reactive oxygen species Reactive Oxygen Species - metabolism ROS, reactive oxygen species SOD, superoxide dismutase Superoxide oxidation TPP+, tetraphenyl phosphonium |
| title | The antioxidant functions of cytochrome c |
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