Multifunctional Cytochrome c: Learning New Tricks from an Old Dog
Cytochrome c (cyt c) is a small soluble heme protein characterized by a relatively flexible structure, particularly in the ferric form, such that it is able to sample a broad conformational space. Depending on the specific conditions, interactions, and cellular localization, different conformations...
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2017
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00092665_v117_n21_p13382_AlvarezPaggi http://hdl.handle.net/20.500.12110/paper_00092665_v117_n21_p13382_AlvarezPaggi |
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paper:paper_00092665_v117_n21_p13382_AlvarezPaggi |
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paper:paper_00092665_v117_n21_p13382_AlvarezPaggi2025-07-30T17:16:53Z Multifunctional Cytochrome c: Learning New Tricks from an Old Dog Binding energy Electric fields Enzyme activity Flexible structures Machinery Phospholipids Phosphorylation Cellular localization Differential properties Moonlighting proteins Oxidative phosphorylation Peroxidase activities Post-translational modifications Technological applications Thermodynamic factors Conformations cytochrome c animal electron transport enzymology genetic procedures human kinetics metabolism mitochondrion oxidation reduction reaction thermodynamics Animals Biosensing Techniques Cytochromes c Electron Transport Humans Kinetics Mitochondria Oxidation-Reduction Thermodynamics Cytochrome c (cyt c) is a small soluble heme protein characterized by a relatively flexible structure, particularly in the ferric form, such that it is able to sample a broad conformational space. Depending on the specific conditions, interactions, and cellular localization, different conformations may be stabilized, which differ in structure, redox properties, binding affinities, and enzymatic activity. The primary function is electron shuttling in oxidative phosphorylation, and is exerted by the so-called native cyt c in the intermembrane mitochondrial space of healthy cells. Under pro-apoptotic conditions, however, cyt c gains cardiolipin peroxidase activity, translocates into the cytosol to engage in the intrinsic apoptotic pathway, and enters the nucleus where it impedes nucleosome assembly. Other reported functions include cytosolic redox sensing and involvement in the mitochondrial oxidative folding machinery. Moreover, post-translational modifications such as nitration, phosphorylation, and sulfoxidation of specific amino acids induce alternative conformations with differential properties, at least in vitro. Similar structural and functional alterations are elicited by biologically significant electric fields and by naturally occurring mutations of human cyt c that, along with mutations at the level of the maturation system, are associated with specific diseases. Here, we summarize current knowledge and recent advances in understanding the different structural, dynamic, and thermodynamic factors that regulate the primary electron transfer function, as well as alternative functions and conformations of cyt c. Finally, we present recent technological applications of this moonlighting protein. © 2017 American Chemical Society. 2017 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00092665_v117_n21_p13382_AlvarezPaggi http://hdl.handle.net/20.500.12110/paper_00092665_v117_n21_p13382_AlvarezPaggi |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Binding energy Electric fields Enzyme activity Flexible structures Machinery Phospholipids Phosphorylation Cellular localization Differential properties Moonlighting proteins Oxidative phosphorylation Peroxidase activities Post-translational modifications Technological applications Thermodynamic factors Conformations cytochrome c animal electron transport enzymology genetic procedures human kinetics metabolism mitochondrion oxidation reduction reaction thermodynamics Animals Biosensing Techniques Cytochromes c Electron Transport Humans Kinetics Mitochondria Oxidation-Reduction Thermodynamics |
| spellingShingle |
Binding energy Electric fields Enzyme activity Flexible structures Machinery Phospholipids Phosphorylation Cellular localization Differential properties Moonlighting proteins Oxidative phosphorylation Peroxidase activities Post-translational modifications Technological applications Thermodynamic factors Conformations cytochrome c animal electron transport enzymology genetic procedures human kinetics metabolism mitochondrion oxidation reduction reaction thermodynamics Animals Biosensing Techniques Cytochromes c Electron Transport Humans Kinetics Mitochondria Oxidation-Reduction Thermodynamics Multifunctional Cytochrome c: Learning New Tricks from an Old Dog |
| topic_facet |
Binding energy Electric fields Enzyme activity Flexible structures Machinery Phospholipids Phosphorylation Cellular localization Differential properties Moonlighting proteins Oxidative phosphorylation Peroxidase activities Post-translational modifications Technological applications Thermodynamic factors Conformations cytochrome c animal electron transport enzymology genetic procedures human kinetics metabolism mitochondrion oxidation reduction reaction thermodynamics Animals Biosensing Techniques Cytochromes c Electron Transport Humans Kinetics Mitochondria Oxidation-Reduction Thermodynamics |
| description |
Cytochrome c (cyt c) is a small soluble heme protein characterized by a relatively flexible structure, particularly in the ferric form, such that it is able to sample a broad conformational space. Depending on the specific conditions, interactions, and cellular localization, different conformations may be stabilized, which differ in structure, redox properties, binding affinities, and enzymatic activity. The primary function is electron shuttling in oxidative phosphorylation, and is exerted by the so-called native cyt c in the intermembrane mitochondrial space of healthy cells. Under pro-apoptotic conditions, however, cyt c gains cardiolipin peroxidase activity, translocates into the cytosol to engage in the intrinsic apoptotic pathway, and enters the nucleus where it impedes nucleosome assembly. Other reported functions include cytosolic redox sensing and involvement in the mitochondrial oxidative folding machinery. Moreover, post-translational modifications such as nitration, phosphorylation, and sulfoxidation of specific amino acids induce alternative conformations with differential properties, at least in vitro. Similar structural and functional alterations are elicited by biologically significant electric fields and by naturally occurring mutations of human cyt c that, along with mutations at the level of the maturation system, are associated with specific diseases. Here, we summarize current knowledge and recent advances in understanding the different structural, dynamic, and thermodynamic factors that regulate the primary electron transfer function, as well as alternative functions and conformations of cyt c. Finally, we present recent technological applications of this moonlighting protein. © 2017 American Chemical Society. |
| title |
Multifunctional Cytochrome c: Learning New Tricks from an Old Dog |
| title_short |
Multifunctional Cytochrome c: Learning New Tricks from an Old Dog |
| title_full |
Multifunctional Cytochrome c: Learning New Tricks from an Old Dog |
| title_fullStr |
Multifunctional Cytochrome c: Learning New Tricks from an Old Dog |
| title_full_unstemmed |
Multifunctional Cytochrome c: Learning New Tricks from an Old Dog |
| title_sort |
multifunctional cytochrome c: learning new tricks from an old dog |
| publishDate |
2017 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00092665_v117_n21_p13382_AlvarezPaggi http://hdl.handle.net/20.500.12110/paper_00092665_v117_n21_p13382_AlvarezPaggi |
| _version_ |
1840324979331170304 |