Alternative Conformations of Cytochrome c: Structure, Function, and Detection

Cytochrome c (cyt c) is a cationic hemoprotein of ∼100 amino acid residues that exhibits exceptional functional versatility. While its primary function is electron transfer in the respiratory chain, cyt c is also recognized as a key component of the intrinsic apoptotic pathway, the mitochondrial oxi...

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Autores principales:	Hannibal, L., Tomasina, F., Capdevila, D.A., Demicheli, V., Tórtora, V., Alvarez-Paggi, D., Jemmerson, R., Murgida, D.H., Radi, R.
Formato:	JOUR
Materias:	Machinery Phospholipids Amino acid residues Cellular compartments Cellular homeostasis Conformational change Conformational state Peroxidase activities Post-translational modifications Structural flexibilities Amino acids cardiolipin cytochrome c methionine peroxidase tyrosine fungal protein phospholipid vegetable protein antigenicity apoptosis cell respiration circular dichroism complex formation conformational transition crystal structure electron transport enzyme activity genetic conservation hydrogen bond immunochemistry in vitro study membrane potential nitration oxidation reduction potential phosphorylation physical chemistry priority journal protein analysis protein conformation protein folding protein function protein phosphorylation protein processing protein secondary structure protein stability protein structure respiratory chain Review static electricity sulfoxidation animal chemistry electricity human intracellular space metabolism protein transport Animals Cardiolipins Cytochromes c Electricity Fungal Proteins Humans Intracellular Space Plant Proteins Protein Conformation Protein Folding Protein Processing, Post-Translational Protein Transport
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_00062960_v55_n3_p407_Hannibal
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_00062960_v55_n3_p407_Hannibal
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spelling	todo:paper_00062960_v55_n3_p407_Hannibal2023-10-03T14:04:37Z Alternative Conformations of Cytochrome c: Structure, Function, and Detection Hannibal, L. Tomasina, F. Capdevila, D.A. Demicheli, V. Tórtora, V. Alvarez-Paggi, D. Jemmerson, R. Murgida, D.H. Radi, R. Machinery Phospholipids Amino acid residues Cellular compartments Cellular homeostasis Conformational change Conformational state Peroxidase activities Post-translational modifications Structural flexibilities Amino acids cardiolipin cytochrome c methionine peroxidase tyrosine cytochrome c fungal protein phospholipid vegetable protein antigenicity apoptosis cell respiration circular dichroism complex formation conformational transition crystal structure electron transport enzyme activity genetic conservation hydrogen bond immunochemistry in vitro study membrane potential nitration oxidation reduction potential phosphorylation physical chemistry priority journal protein analysis protein conformation protein folding protein function protein phosphorylation protein processing protein secondary structure protein stability protein structure respiratory chain Review static electricity sulfoxidation animal chemistry electricity human intracellular space metabolism protein conformation protein transport Animals Cardiolipins Cytochromes c Electricity Fungal Proteins Humans Intracellular Space Phospholipids Plant Proteins Protein Conformation Protein Folding Protein Processing, Post-Translational Protein Transport Cytochrome c (cyt c) is a cationic hemoprotein of ∼100 amino acid residues that exhibits exceptional functional versatility. While its primary function is electron transfer in the respiratory chain, cyt c is also recognized as a key component of the intrinsic apoptotic pathway, the mitochondrial oxidative protein folding machinery, and presumably as a redox sensor in the cytosol, along with other reported functions. Transition to alternative conformations and gain-of-peroxidase activity are thought to further enable the multiple functions of cyt c and its translocation across cellular compartments. In vitro, direct interactions of cyt c with cardiolipin, post-translational modifications such as tyrosine nitration, phosphorylation, methionine sulfoxidation, mutations, and even fine changes in electrical fields lead to a variety of conformational states that may be of biological relevance. The identification of these alternative conformations and the elucidation of their functions in vivo continue to be a major challenge. Here, we unify the knowledge of the structural flexibility of cyt c that supports functional moonlighting and review biochemical and immunochemical evidence confirming that cyt c undergoes conformational changes during normal and altered cellular homeostasis. © 2015 American Chemical Society. Fil:Capdevila, D.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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00062960_v55_n3_p407_Hannibal
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Machinery Phospholipids Amino acid residues Cellular compartments Cellular homeostasis Conformational change Conformational state Peroxidase activities Post-translational modifications Structural flexibilities Amino acids cardiolipin cytochrome c methionine peroxidase tyrosine cytochrome c fungal protein phospholipid vegetable protein antigenicity apoptosis cell respiration circular dichroism complex formation conformational transition crystal structure electron transport enzyme activity genetic conservation hydrogen bond immunochemistry in vitro study membrane potential nitration oxidation reduction potential phosphorylation physical chemistry priority journal protein analysis protein conformation protein folding protein function protein phosphorylation protein processing protein secondary structure protein stability protein structure respiratory chain Review static electricity sulfoxidation animal chemistry electricity human intracellular space metabolism protein conformation protein transport Animals Cardiolipins Cytochromes c Electricity Fungal Proteins Humans Intracellular Space Phospholipids Plant Proteins Protein Conformation Protein Folding Protein Processing, Post-Translational Protein Transport
spellingShingle	Machinery Phospholipids Amino acid residues Cellular compartments Cellular homeostasis Conformational change Conformational state Peroxidase activities Post-translational modifications Structural flexibilities Amino acids cardiolipin cytochrome c methionine peroxidase tyrosine cytochrome c fungal protein phospholipid vegetable protein antigenicity apoptosis cell respiration circular dichroism complex formation conformational transition crystal structure electron transport enzyme activity genetic conservation hydrogen bond immunochemistry in vitro study membrane potential nitration oxidation reduction potential phosphorylation physical chemistry priority journal protein analysis protein conformation protein folding protein function protein phosphorylation protein processing protein secondary structure protein stability protein structure respiratory chain Review static electricity sulfoxidation animal chemistry electricity human intracellular space metabolism protein conformation protein transport Animals Cardiolipins Cytochromes c Electricity Fungal Proteins Humans Intracellular Space Phospholipids Plant Proteins Protein Conformation Protein Folding Protein Processing, Post-Translational Protein Transport Hannibal, L. Tomasina, F. Capdevila, D.A. Demicheli, V. Tórtora, V. Alvarez-Paggi, D. Jemmerson, R. Murgida, D.H. Radi, R. Alternative Conformations of Cytochrome c: Structure, Function, and Detection
topic_facet	Machinery Phospholipids Amino acid residues Cellular compartments Cellular homeostasis Conformational change Conformational state Peroxidase activities Post-translational modifications Structural flexibilities Amino acids cardiolipin cytochrome c methionine peroxidase tyrosine cytochrome c fungal protein phospholipid vegetable protein antigenicity apoptosis cell respiration circular dichroism complex formation conformational transition crystal structure electron transport enzyme activity genetic conservation hydrogen bond immunochemistry in vitro study membrane potential nitration oxidation reduction potential phosphorylation physical chemistry priority journal protein analysis protein conformation protein folding protein function protein phosphorylation protein processing protein secondary structure protein stability protein structure respiratory chain Review static electricity sulfoxidation animal chemistry electricity human intracellular space metabolism protein conformation protein transport Animals Cardiolipins Cytochromes c Electricity Fungal Proteins Humans Intracellular Space Phospholipids Plant Proteins Protein Conformation Protein Folding Protein Processing, Post-Translational Protein Transport
description	Cytochrome c (cyt c) is a cationic hemoprotein of ∼100 amino acid residues that exhibits exceptional functional versatility. While its primary function is electron transfer in the respiratory chain, cyt c is also recognized as a key component of the intrinsic apoptotic pathway, the mitochondrial oxidative protein folding machinery, and presumably as a redox sensor in the cytosol, along with other reported functions. Transition to alternative conformations and gain-of-peroxidase activity are thought to further enable the multiple functions of cyt c and its translocation across cellular compartments. In vitro, direct interactions of cyt c with cardiolipin, post-translational modifications such as tyrosine nitration, phosphorylation, methionine sulfoxidation, mutations, and even fine changes in electrical fields lead to a variety of conformational states that may be of biological relevance. The identification of these alternative conformations and the elucidation of their functions in vivo continue to be a major challenge. Here, we unify the knowledge of the structural flexibility of cyt c that supports functional moonlighting and review biochemical and immunochemical evidence confirming that cyt c undergoes conformational changes during normal and altered cellular homeostasis. © 2015 American Chemical Society.
format	JOUR
author	Hannibal, L. Tomasina, F. Capdevila, D.A. Demicheli, V. Tórtora, V. Alvarez-Paggi, D. Jemmerson, R. Murgida, D.H. Radi, R.
author_facet	Hannibal, L. Tomasina, F. Capdevila, D.A. Demicheli, V. Tórtora, V. Alvarez-Paggi, D. Jemmerson, R. Murgida, D.H. Radi, R.
author_sort	Hannibal, L.
title	Alternative Conformations of Cytochrome c: Structure, Function, and Detection
title_short	Alternative Conformations of Cytochrome c: Structure, Function, and Detection
title_full	Alternative Conformations of Cytochrome c: Structure, Function, and Detection
title_fullStr	Alternative Conformations of Cytochrome c: Structure, Function, and Detection
title_full_unstemmed	Alternative Conformations of Cytochrome c: Structure, Function, and Detection
title_sort	alternative conformations of cytochrome c: structure, function, and detection
url	http://hdl.handle.net/20.500.12110/paper_00062960_v55_n3_p407_Hannibal
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Alternative Conformations of Cytochrome c: Structure, Function, and Detection

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