Gast ::
| Hauptseite > Publikationsdatenbank > Heterolytic reduction of fatty acid hydroperoxides by cytochrome c/cardiolipin complexes: antioxidant function in mitochondria > print |
| Hauptseite > Publikationsdatenbank > Heterolytic reduction of fatty acid hydroperoxides by cytochrome c/cardiolipin complexes: antioxidant function in mitochondria > print |
| 001 | 7755 | ||
| 005 | 20200402205740.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:19627079 |
| 024 | 7 | _ | |2 DOI |a 10.1021/ja904343c |
| 024 | 7 | _ | |2 WOS |a WOS:000269379200009 |
| 024 | 7 | _ | |a altmetric:21803352 |2 altmetric |
| 037 | _ | _ | |a PreJuSER-7755 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 540 |
| 084 | _ | _ | |2 WoS |a Chemistry, Multidisciplinary |
| 100 | 1 | _ | |0 P:(DE-HGF)0 |a Belikova, N.A. |b 0 |
| 245 | _ | _ | |a Heterolytic reduction of fatty acid hydroperoxides by cytochrome c/cardiolipin complexes: antioxidant function in mitochondria |
| 260 | _ | _ | |a Washington, DC |b American Chemical Society |c 2009 |
| 300 | _ | _ | |a 11288 - 11289 |
| 336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a article |2 DRIVER |
| 440 | _ | 0 | |0 8502 |a Journal of the American Chemical Society |v 131 |x 0002-7863 |y 32 |
| 500 | _ | _ | |a This work was supported by grants from the NIH (U19-AI068021, HL70755, R03TW007320, 2RO1LM007994-05), the NSF (CC0449117), the PittGrid, and la Junta de Extremadura, Orden 2008050288 (A.K.S.A.). |
| 520 | _ | _ | |a Cytochrome c (cyt c), a mitochondrial intermembrane electron shuttle between complexes III and IV, can, upon binding with an anionic phospholipid, cardiolipin (CL), act as a peroxidase that catalyzes cardiolipin oxidation. H(2)O(2) was considered as a source of oxidative equivalents for this reaction, which is essential for programmed cell death. Here we report that peroxidase cyt c/CL complexes can utilize free fatty acid hydroperoxides (FFA-OOH) at exceptionally high rates that are approximately 3 orders of magnitude higher than for H(2)O(2). Similarly, peroxidase activity of murine liver mitochondria was high with FFA-OOH. Using EPR spin trapping and LC-MS techniques, we have demonstrated that cyt c/CL complexes split FFA-OOH predominantly via a heterolytic mechanism, yielding hydroxy-fatty acids, whereas H(2)O(2) (and tert-butyl hydroperoxide, t-BuOOH) undergo homolytic cleavage. Computer simulations have revealed that Arg(38) and His(33) are important for the heterolytic mechanism at potential FFA-OOH binding sites of cyt c (but not for H(2)O(2) or t-BuOOH). Regulation of FFA-OOH metabolism may be an important function of cyt c that is associated with elimination of toxic FFA-OOH and synthesis of physiologically active hydroxy-fatty acids in mitochondria. |
| 536 | _ | _ | |0 G:(DE-Juel1)FUEK443 |2 G:(DE-HGF) |a Programm Biosoft |c N03 |x 0 |
| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a Animals |
| 650 | _ | 2 | |2 MeSH |a Antioxidants: metabolism |
| 650 | _ | 2 | |2 MeSH |a Armoracia: enzymology |
| 650 | _ | 2 | |2 MeSH |a Cardiolipins: metabolism |
| 650 | _ | 2 | |2 MeSH |a Cytochromes c: metabolism |
| 650 | _ | 2 | |2 MeSH |a Fatty Acids: metabolism |
| 650 | _ | 2 | |2 MeSH |a Hydrogen Peroxide: metabolism |
| 650 | _ | 2 | |2 MeSH |a Mitochondria, Liver: enzymology |
| 650 | _ | 2 | |2 MeSH |a Models, Molecular |
| 650 | _ | 2 | |2 MeSH |a Murinae |
| 650 | _ | 2 | |2 MeSH |a Oxidation-Reduction |
| 650 | _ | 2 | |2 MeSH |a Protein Binding |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Antioxidants |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Cardiolipins |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Fatty Acids |
| 650 | _ | 7 | |0 7722-84-1 |2 NLM Chemicals |a Hydrogen Peroxide |
| 650 | _ | 7 | |0 9007-43-6 |2 NLM Chemicals |a Cytochromes c |
| 650 | _ | 7 | |2 WoSType |a J |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Tyurina, Y.Y. |b 1 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Borisenko, G. |b 2 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Tyurin, V. |b 3 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Samhan Arias, A.K. |b 4 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Yanamala, N. |b 5 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Furtmüller, P.G. |b 6 |
| 700 | 1 | _ | |0 P:(DE-Juel1)VDB44599 |a Klein-Seetharaman, J. |b 7 |u FZJ |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Obinger, C. |b 8 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Kagan, V.E. |b 9 |
| 773 | _ | _ | |0 PERI:(DE-600)1472210-0 |a 10.1021/ja904343c |g Vol. 131, p. 11288 - 11289 |p 11288 - 11289 |q 131<11288 - 11289 |t Journal of the American Chemical Society |v 131 |x 0002-7863 |y 2009 |
| 856 | 7 | _ | |u http://dx.doi.org/10.1021/ja904343c |
| 909 | C | O | |o oai:juser.fz-juelich.de:7755 |p VDB |
| 913 | 1 | _ | |0 G:(DE-Juel1)FUEK443 |a DE-HGF |b Schlüsseltechnologien |k N03 |l BioSoft |v Programm Biosoft |x 0 |z entfällt |
| 914 | 1 | _ | |y 2009 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
| 920 | 1 | _ | |0 I:(DE-Juel1)ISB-2-20090406 |d 31.12.2010 |g ISB |k ISB-2 |l Molekulare Biophysik |x 0 |
| 970 | _ | _ | |a VDB:(DE-Juel1)116458 |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a ConvertedRecord |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
| 980 | _ | _ | |a UNRESTRICTED |
| 981 | _ | _ | |a I:(DE-Juel1)IBI-7-20200312 |
| 981 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
| 981 | _ | _ | |a I:(DE-Juel1)ISB-2-20090406 |
| Library | Collection | CLSMajor | CLSMinor | Language | Author |
|---|