Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: Potential implications for apoptosis
Cytochrome c (Cyt-c) has been previously shown to participate in cardiolipin (CL) oxidation and, therefore, in mitochondrial membrane permeabilization during the early events of apoptosis. The gain in this function has been ascribed to specific CL/Cyt-c interactions. Here we report that the cationic...
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_20416520_v6_n1_p705_Capdevila http://hdl.handle.net/20.500.12110/paper_20416520_v6_n1_p705_Capdevila |
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paper:paper_20416520_v6_n1_p705_Capdevila2023-06-08T16:33:12Z Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: Potential implications for apoptosis Capdevila, Daiana Andrea Marmisolle, Waldemar Alejandro Murgida, Daniel Horacio Amino acids Bins Cell death Cell membranes Lipids Mitochondria Oxidation Phospholipids Proteins Activated proteins Cationic proteins Membrane components Methionine oxidation Mitochondrial membranes Phosphatidylcholine Phosphatidylethanolamine Zwitterionic lipids C (programming language) Cytochrome c (Cyt-c) has been previously shown to participate in cardiolipin (CL) oxidation and, therefore, in mitochondrial membrane permeabilization during the early events of apoptosis. The gain in this function has been ascribed to specific CL/Cyt-c interactions. Here we report that the cationic protein Cyt-c is also able to interact electrostatically with the main lipid components of the mitochondrial membranes, the zwitterionic lipids phosphatidylcholine (PC) and phosphatidylethanolamine (PE), through the mediation of phosphate anions that bind specifically to amino groups in the surfaces of protein and model membranes. In these complexes, Cyt-c reacts efficiently with H 2 O 2 at submillimolar levels, which oxidizes the sulfur atom of the axial ligand Met80. The modified protein is stable and presents significantly enhanced peroxidatic activity. Based on these results, we postulate that the rise of H 2 O 2 concentrations to the submillimolar levels registered during initiation of the apoptotic program may represent one signaling event that triggers the gain in peroxidatic function of the Cyt-c molecules bound to the abundant PE and PC membrane components. As the activated protein is a chemically stable species, it can potentially bind and oxidize important targets, such as CL. This journal is © The Royal Society of Chemistry. Fil:Capdevila, D.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Marmisollé, W.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Murgida, D.H. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2015 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_20416520_v6_n1_p705_Capdevila http://hdl.handle.net/20.500.12110/paper_20416520_v6_n1_p705_Capdevila |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Amino acids Bins Cell death Cell membranes Lipids Mitochondria Oxidation Phospholipids Proteins Activated proteins Cationic proteins Membrane components Methionine oxidation Mitochondrial membranes Phosphatidylcholine Phosphatidylethanolamine Zwitterionic lipids C (programming language) |
| spellingShingle |
Amino acids Bins Cell death Cell membranes Lipids Mitochondria Oxidation Phospholipids Proteins Activated proteins Cationic proteins Membrane components Methionine oxidation Mitochondrial membranes Phosphatidylcholine Phosphatidylethanolamine Zwitterionic lipids C (programming language) Capdevila, Daiana Andrea Marmisolle, Waldemar Alejandro Murgida, Daniel Horacio Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: Potential implications for apoptosis |
| topic_facet |
Amino acids Bins Cell death Cell membranes Lipids Mitochondria Oxidation Phospholipids Proteins Activated proteins Cationic proteins Membrane components Methionine oxidation Mitochondrial membranes Phosphatidylcholine Phosphatidylethanolamine Zwitterionic lipids C (programming language) |
| description |
Cytochrome c (Cyt-c) has been previously shown to participate in cardiolipin (CL) oxidation and, therefore, in mitochondrial membrane permeabilization during the early events of apoptosis. The gain in this function has been ascribed to specific CL/Cyt-c interactions. Here we report that the cationic protein Cyt-c is also able to interact electrostatically with the main lipid components of the mitochondrial membranes, the zwitterionic lipids phosphatidylcholine (PC) and phosphatidylethanolamine (PE), through the mediation of phosphate anions that bind specifically to amino groups in the surfaces of protein and model membranes. In these complexes, Cyt-c reacts efficiently with H 2 O 2 at submillimolar levels, which oxidizes the sulfur atom of the axial ligand Met80. The modified protein is stable and presents significantly enhanced peroxidatic activity. Based on these results, we postulate that the rise of H 2 O 2 concentrations to the submillimolar levels registered during initiation of the apoptotic program may represent one signaling event that triggers the gain in peroxidatic function of the Cyt-c molecules bound to the abundant PE and PC membrane components. As the activated protein is a chemically stable species, it can potentially bind and oxidize important targets, such as CL. This journal is © The Royal Society of Chemistry. |
| author |
Capdevila, Daiana Andrea Marmisolle, Waldemar Alejandro Murgida, Daniel Horacio |
| author_facet |
Capdevila, Daiana Andrea Marmisolle, Waldemar Alejandro Murgida, Daniel Horacio |
| author_sort |
Capdevila, Daiana Andrea |
| title |
Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: Potential implications for apoptosis |
| title_short |
Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: Potential implications for apoptosis |
| title_full |
Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: Potential implications for apoptosis |
| title_fullStr |
Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: Potential implications for apoptosis |
| title_full_unstemmed |
Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: Potential implications for apoptosis |
| title_sort |
specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: potential implications for apoptosis |
| publishDate |
2015 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_20416520_v6_n1_p705_Capdevila http://hdl.handle.net/20.500.12110/paper_20416520_v6_n1_p705_Capdevila |
| work_keys_str_mv |
AT capdeviladaianaandrea specificmethionineoxidationofcytochromecincomplexeswithzwitterioniclipidsbyhydrogenperoxidepotentialimplicationsforapoptosis AT marmisollewaldemaralejandro specificmethionineoxidationofcytochromecincomplexeswithzwitterioniclipidsbyhydrogenperoxidepotentialimplicationsforapoptosis AT murgidadanielhoracio specificmethionineoxidationofcytochromecincomplexeswithzwitterioniclipidsbyhydrogenperoxidepotentialimplicationsforapoptosis |
| _version_ |
1768543535417524224 |