Difference between revisions of "Capdevila 2015 Biochemistry"
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{{Publication | {{Publication | ||
|title=Capdevila DA, Oviedo Rouco S, Tomasina F, Tortora V, Demicheli V, Radi R, Murgida DH (2015) Active site structure and peroxidase activity of oxidatively modified cytochrome c species in complexes with cardiolipin. Biochemistry 54:7491-504. | |title=Capdevila DA, Oviedo Rouco S, Tomasina F, Tortora V, Demicheli V, Radi R, Murgida DH (2015) Active site structure and peroxidase activity of oxidatively modified cytochrome c species in complexes with cardiolipin. Biochemistry 54:7491-504. | ||
|info=[http://www.ncbi.nlm.nih.gov/pubmed/26620444 PMID: 26620444] | |info=[http://www.ncbi.nlm.nih.gov/pubmed/26620444 PMID: 26620444] | ||
|authors=Capdevila DA, Oviedo Rouco S, Tomasina F, Tortora V, Demicheli V, Radi R, Murgida DH | |authors=Capdevila DA, Oviedo Rouco S, Tomasina F, Tortora V, Demicheli V, Radi R, Murgida DH | ||
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|journal=Biochemistry | |journal=Biochemistry | ||
|abstract=We report a resonance Raman and UV-vis characterization of the active site structure of oxidatively modified forms of cytochrome c (Cyt-c) free in solution and in complexes with cardiolipin (CL). The studied post-translational modifications of Cyt-c include methionine sulfoxidation and tyrosine nitration, which lead to altered heme axial ligation and increased peroxidase activity with respect to those of the wild-type protein. In spite of the structural and activity differences between the protein variants free in solution, binding to CL liposomes induces in all cases the formation of a spectroscopically identical bis-His axial coordination conformer that more efficiently promotes lipid peroxidation. The spectroscopic results indicate that the bis-His form is in equilibrium with small amounts of high-spin species, thus suggesting a labile distal His ligand as the basis for the CL-induced increase in enzymatic activity observed for all protein variants. For Cyt-c nitrated at Tyr74 and sulfoxidized at Met80, the measured apparent binding affinities for CL are ∼4 times larger than for wild-type Cyt-c. On the basis of these results, we propose that these post-translational modifications may amplify the pro-apoptotic signal of Cyt-c under oxidative stress conditions at CL concentrations lower than for the unmodified protein. | |abstract=We report a resonance Raman and UV-vis characterization of the active site structure of oxidatively modified forms of cytochrome c (Cyt-c) free in solution and in complexes with cardiolipin (CL). The studied post-translational modifications of Cyt-c include methionine sulfoxidation and tyrosine nitration, which lead to altered heme axial ligation and increased peroxidase activity with respect to those of the wild-type protein. In spite of the structural and activity differences between the protein variants free in solution, binding to CL liposomes induces in all cases the formation of a spectroscopically identical bis-His axial coordination conformer that more efficiently promotes lipid peroxidation. The spectroscopic results indicate that the bis-His form is in equilibrium with small amounts of high-spin species, thus suggesting a labile distal His ligand as the basis for the CL-induced increase in enzymatic activity observed for all protein variants. For Cyt-c nitrated at Tyr74 and sulfoxidized at Met80, the measured apparent binding affinities for CL are ∼4 times larger than for wild-type Cyt-c. On the basis of these results, we propose that these post-translational modifications may amplify the pro-apoptotic signal of Cyt-c under oxidative stress conditions at CL concentrations lower than for the unmodified protein. | ||
|keywords=Amplex Red | |keywords=Amplex Red, Cytochrome c, Liposome | ||
|mipnetlab=UY Montevideo Radi R | |mipnetlab=UY Montevideo Radi R | ||
}} | }} | ||
{{Labeling | {{Labeling | ||
|area=Respiration | |area=Respiration, Genetic knockout;overexpression | ||
|tissues=Fat | |tissues=Fat | ||
|topics=Cyt c | |topics=Cyt c | ||
|instruments=Oxygraph-2k | |instruments=Oxygraph-2k | ||
|additional= | |additional=2016-01 | ||
}} | }} | ||
Latest revision as of 16:40, 11 February 2016
| Capdevila DA, Oviedo Rouco S, Tomasina F, Tortora V, Demicheli V, Radi R, Murgida DH (2015) Active site structure and peroxidase activity of oxidatively modified cytochrome c species in complexes with cardiolipin. Biochemistry 54:7491-504. |
Capdevila DA, Oviedo Rouco S, Tomasina F, Tortora V, Demicheli V, Radi R, Murgida DH (2015) Biochemistry
Abstract: We report a resonance Raman and UV-vis characterization of the active site structure of oxidatively modified forms of cytochrome c (Cyt-c) free in solution and in complexes with cardiolipin (CL). The studied post-translational modifications of Cyt-c include methionine sulfoxidation and tyrosine nitration, which lead to altered heme axial ligation and increased peroxidase activity with respect to those of the wild-type protein. In spite of the structural and activity differences between the protein variants free in solution, binding to CL liposomes induces in all cases the formation of a spectroscopically identical bis-His axial coordination conformer that more efficiently promotes lipid peroxidation. The spectroscopic results indicate that the bis-His form is in equilibrium with small amounts of high-spin species, thus suggesting a labile distal His ligand as the basis for the CL-induced increase in enzymatic activity observed for all protein variants. For Cyt-c nitrated at Tyr74 and sulfoxidized at Met80, the measured apparent binding affinities for CL are ∼4 times larger than for wild-type Cyt-c. On the basis of these results, we propose that these post-translational modifications may amplify the pro-apoptotic signal of Cyt-c under oxidative stress conditions at CL concentrations lower than for the unmodified protein. • Keywords: Amplex Red, Cytochrome c, Liposome
• O2k-Network Lab: UY Montevideo Radi R
Labels: MiParea: Respiration, Genetic knockout;overexpression
Tissue;cell: Fat
Regulation: Cyt c
HRR: Oxygraph-2k
2016-01
