Cytochrome c (Cyt c) has been widely used as a model protein for electron transfer studies, due to its unique characteristics and electrochemical properties. It is known that electron transfer reactions are directly influenced by the way the protein is immobilized on electrode surfaces. In this context, different immobilization strategies and ...
A Case Study of Cytochrome c
Cytochrome c (Cyt c) has been widely used as a model protein for electron transfer studies, due to its unique characteristics and electrochemical properties. It is known that electron transfer ...
A Case Study of Cytochrome c
A Case Study of Cytochrome c 37 2 Cytochrome c, a Brief Understanding The Cyt c is a cationic highly water-soluble protein, with approximately spherical shape (relatively diameter small of 3.4 nm), containing a prosthetic group formed by the porphyrin complex of heme (Fe2+) and amino acid residues (often cysteine,
Cytochrome c : functions beyond respiration
Cytochrome c is one of the mitochondrial proteins that is released into the cytosol when the cell is activated by an apoptotic stimulus. In the cytosol, cytochrome c engages the apoptotic protease ...
Diverse functions of cytochrome c in cell death and disease
The redox-active protein cytochrome c is a highly positively charged hemoglobin that regulates cell fate decisions of life and death. Under normal physiological conditions, cytochrome c is ...
PDF Diverse functions of cytochrome c in cell death and disease
All these structural studies highlight cytochrome c's multifunctionality in both apoptosis and cellular respiration. Z. Zhou et al. 388 Cell Death & Differentiation (2024) 31:387-404.
Cytochrome c as an experimental model protein
Cytochrome c was a primary candidate for studies of molecular evolution. Numerous cytochrome c polypeptides had been sequenced four decades ago giving an early set of data on which to perform analyses of phylogenetics and sequence conservation. 11, 12 It was one of the first proteins to be studied by site-directed mutagenesis 13 for the same reason. Because of its occurrence in organelles ...
Cytochrome c: An extreme multifunctional protein with a key role in
Cytochrome c, a protein that belongs to class 1 of the c-type cytochrome family, exerts different functions depending on its cellular localization and the conditions in which it operates; therefore, it can be defined as 'extreme multifunctional' protein. It mediates electron-transfer in the respiratory chain and acts as a detoxifying agent to dispose of ROS.
A Case Study of Cytochrome c
Wang, G.-X., et al.: Heme plane orientation dependent direct electron transfer of cytochrome c at SAMs/Au electrodes with different wettability. Chem. Commun. 48(88), 10859-10861 (2012)
PDF Dual Targeting of a Mitochondrial Protein: The Case Study of Cytochrome c1
Case Study of Cytochrome c 1 Anja Ro¨diger, Bianca Baudisch, Uwe Langner and Ralf Bernd Klo¨sgen1 Institute of Biology—Plant Physiology, Martin Luther University Halle-Wittenberg, Weinbergweg 10, 06120 Halle/Saale, Germany ABSTRACT As a result of the endosymbiotic gene transfer, the majority of proteins of mitochondria and chloroplasts is
Cytochrome C
Cytochrome c. H. Tuppy, G. Kreil, in Encyclopedia of Biological Chemistry (Second Edition), 2013 Abstract. Cytochrome c is a heme protein that is present in and can easily be isolated from mitochondria of all eukaryotic organisms. The amino acid sequence of the protein moiety was among the first sequences that could be elucidated. This was the starting point for comparative studies about ...
In-silico assessment of protein-protein electron transfer. a case study
In-silico assessment of protein-protein electron transfer. a case study: cytochrome c peroxidase--cytochrome c PLoS Comput Biol. 2013;9(3): e1002990. ... We performed a quantitative study of the ET between Cytochrome c Peroxidase and its redox partner Cytochrome c. Our results confirm the ET mechanism as hole transfer (HT) through residues ...
Frontiers
All studies converge to the fact that in case of cell apoptosis or necrosis cytochrome c is released from the mitochondria into the extracellular space. Many studies confirmed that serum cytochrome c can be easily measured and used for diagnosing and assessing the severity of pathological entities characterized by cell death. However, different studies have shown diverse serum cytochrome c ...
Factors defining effects of macromolecular crowding on protein ...
Factors defining effects of macromolecular crowding on protein stability: an in vitro/in silico case study using cytochrome c Biochemistry. 2010 Aug 10;49(31):6519-30. doi: 10.1021/bi100578x. ... In silico analysis, using structure-based (Go-like) interactions for cytochrome c, is in excellent agreement with the in vitro thermodynamic data and ...
Influence of Structured Water Layers on Protein Adsorption Process: A
Cytochrome c, an essential protein of the electron transport chain, is known to be capable of amplifying the toxicity of carbon nanomaterials via free-radical generation. To understand their interaction, as well as the more general protein-nanoparticle interaction at molecular levels, we investigate the adsorptions between cytochrome c and carbon nanotubes (CNTs) in dynamic and thermodynamic ...
Cytochrome c: An extreme multifunctional protein with a key role in
Cytochrome c, a protein that belongs to class 1 of the c-type cytochrome family, exerts different functions depending on its cellular localization and the conditions in which it operates; therefore, it can be defined as 'extreme multifunctional' protein.It mediates electron-transfer in the respiratory chain and acts as a detoxifying agent to dispose of ROS.
Hydrogen/Deuterium Exchange Measurements May Provide an ...
Hydrogen/Deuterium Exchange Measurements May Provide an Incomplete View of Protein Dynamics: a Case Study on Cytochrome c. Anal Chem. 2021 Oct 26;93(42):14121-14129. doi: 10.1021/acs.analchem.1c02471. Epub 2021 Oct 13. ... We explore this issue in experiments on cytochrome c (cyt c). Compared to the Fe(II) protein, Fe ...
A new quantitative assay for cytochrome c release in apoptotic cells
Cytochrome c then triggers activation of caspase proteases via the formation of a complex known as apoptosome ... In each case, the apoptotic and ... A time course study revealed that the number ...
PDF Microsoft Word
Incomplete View of Protein Dynamics: A Case Study on Cytochrome c Pablo M. Scrosati, Victor Yin, and Lars Konermann* Department of Chemistry, The University of Western Ontario, London, Ontario N6A 5B7, Canada * corresponding author: [email protected] This file contains: Complete Methods Section Figure S1: UV-Vis and MS characterization of cyt c ...
Implementation of cytochrome c proteins and carbon nanotubes ...
Multiheme cytochrome c (Cyt c) can function as a redox protein on electrode to accomplish bioelectrocatalysis. However, the direct electron transfer (DET) between the redox site of Cyt c and electrode is low due to the large coupling distance. A close proximity or a connection pathway from the deeply buried active site to the protein surface can be established by modifying the electrode with ...
Hydrogen/Deuterium Exchange Measurements May Provide an ...
Finally, in a study of cytochrome c, Scrosati et al. use HDX-MS data and MD simulations to explain differences in deuteration patterns between the Fe(II) and Fe(III) species.
Cryopreservation of Proteins Using Ionic Liquids: A Case Study of
Aqueous ionic liquid (IL) solutions form a glassy state at 77 K over a wide concentration of ILs. They have potential as novel cryopreservation/refolding solvents for proteins. However, even if proteins in glass-forming concentrations of ILs are preserved at 77 K, the recovery of activity and the structure of the proteins after cryopreservation are still unclear. To achieve high recovery of ...
ChemElectroChem
Direct electron transfer between cytochrome c and nanostar-coated pyrolytic graphite electrodes was observed with the protein in solution. The electrochemical response was improved at nanostars functionalized with a 1 : 1 mixture of 11-mercaptoundecanoic acid and 4-mercaptobenzoic acid in comparison with gold nanospheres coated with a similar ...
COMMENTS
Cytochrome c (Cyt c) has been widely used as a model protein for electron transfer studies, due to its unique characteristics and electrochemical properties. It is known that electron transfer reactions are directly influenced by the way the protein is immobilized on electrode surfaces. In this context, different immobilization strategies and ...
Cytochrome c (Cyt c) has been widely used as a model protein for electron transfer studies, due to its unique characteristics and electrochemical properties. It is known that electron transfer ...
A Case Study of Cytochrome c 37 2 Cytochrome c, a Brief Understanding The Cyt c is a cationic highly water-soluble protein, with approximately spherical shape (relatively diameter small of 3.4 nm), containing a prosthetic group formed by the porphyrin complex of heme (Fe2+) and amino acid residues (often cysteine,
Cytochrome c is one of the mitochondrial proteins that is released into the cytosol when the cell is activated by an apoptotic stimulus. In the cytosol, cytochrome c engages the apoptotic protease ...
The redox-active protein cytochrome c is a highly positively charged hemoglobin that regulates cell fate decisions of life and death. Under normal physiological conditions, cytochrome c is ...
All these structural studies highlight cytochrome c's multifunctionality in both apoptosis and cellular respiration. Z. Zhou et al. 388 Cell Death & Differentiation (2024) 31:387-404.
Cytochrome c was a primary candidate for studies of molecular evolution. Numerous cytochrome c polypeptides had been sequenced four decades ago giving an early set of data on which to perform analyses of phylogenetics and sequence conservation. 11, 12 It was one of the first proteins to be studied by site-directed mutagenesis 13 for the same reason. Because of its occurrence in organelles ...
Cytochrome c, a protein that belongs to class 1 of the c-type cytochrome family, exerts different functions depending on its cellular localization and the conditions in which it operates; therefore, it can be defined as 'extreme multifunctional' protein. It mediates electron-transfer in the respiratory chain and acts as a detoxifying agent to dispose of ROS.
Wang, G.-X., et al.: Heme plane orientation dependent direct electron transfer of cytochrome c at SAMs/Au electrodes with different wettability. Chem. Commun. 48(88), 10859-10861 (2012)
Case Study of Cytochrome c 1 Anja Ro¨diger, Bianca Baudisch, Uwe Langner and Ralf Bernd Klo¨sgen1 Institute of Biology—Plant Physiology, Martin Luther University Halle-Wittenberg, Weinbergweg 10, 06120 Halle/Saale, Germany ABSTRACT As a result of the endosymbiotic gene transfer, the majority of proteins of mitochondria and chloroplasts is
Cytochrome c. H. Tuppy, G. Kreil, in Encyclopedia of Biological Chemistry (Second Edition), 2013 Abstract. Cytochrome c is a heme protein that is present in and can easily be isolated from mitochondria of all eukaryotic organisms. The amino acid sequence of the protein moiety was among the first sequences that could be elucidated. This was the starting point for comparative studies about ...
In-silico assessment of protein-protein electron transfer. a case study: cytochrome c peroxidase--cytochrome c PLoS Comput Biol. 2013;9(3): e1002990. ... We performed a quantitative study of the ET between Cytochrome c Peroxidase and its redox partner Cytochrome c. Our results confirm the ET mechanism as hole transfer (HT) through residues ...
All studies converge to the fact that in case of cell apoptosis or necrosis cytochrome c is released from the mitochondria into the extracellular space. Many studies confirmed that serum cytochrome c can be easily measured and used for diagnosing and assessing the severity of pathological entities characterized by cell death. However, different studies have shown diverse serum cytochrome c ...
Factors defining effects of macromolecular crowding on protein stability: an in vitro/in silico case study using cytochrome c Biochemistry. 2010 Aug 10;49(31):6519-30. doi: 10.1021/bi100578x. ... In silico analysis, using structure-based (Go-like) interactions for cytochrome c, is in excellent agreement with the in vitro thermodynamic data and ...
Cytochrome c, an essential protein of the electron transport chain, is known to be capable of amplifying the toxicity of carbon nanomaterials via free-radical generation. To understand their interaction, as well as the more general protein-nanoparticle interaction at molecular levels, we investigate the adsorptions between cytochrome c and carbon nanotubes (CNTs) in dynamic and thermodynamic ...
Cytochrome c, a protein that belongs to class 1 of the c-type cytochrome family, exerts different functions depending on its cellular localization and the conditions in which it operates; therefore, it can be defined as 'extreme multifunctional' protein.It mediates electron-transfer in the respiratory chain and acts as a detoxifying agent to dispose of ROS.
Hydrogen/Deuterium Exchange Measurements May Provide an Incomplete View of Protein Dynamics: a Case Study on Cytochrome c. Anal Chem. 2021 Oct 26;93(42):14121-14129. doi: 10.1021/acs.analchem.1c02471. Epub 2021 Oct 13. ... We explore this issue in experiments on cytochrome c (cyt c). Compared to the Fe(II) protein, Fe ...
Cytochrome c then triggers activation of caspase proteases via the formation of a complex known as apoptosome ... In each case, the apoptotic and ... A time course study revealed that the number ...
Incomplete View of Protein Dynamics: A Case Study on Cytochrome c Pablo M. Scrosati, Victor Yin, and Lars Konermann* Department of Chemistry, The University of Western Ontario, London, Ontario N6A 5B7, Canada * corresponding author: [email protected] This file contains: Complete Methods Section Figure S1: UV-Vis and MS characterization of cyt c ...
Multiheme cytochrome c (Cyt c) can function as a redox protein on electrode to accomplish bioelectrocatalysis. However, the direct electron transfer (DET) between the redox site of Cyt c and electrode is low due to the large coupling distance. A close proximity or a connection pathway from the deeply buried active site to the protein surface can be established by modifying the electrode with ...
Finally, in a study of cytochrome c, Scrosati et al. use HDX-MS data and MD simulations to explain differences in deuteration patterns between the Fe(II) and Fe(III) species.
Aqueous ionic liquid (IL) solutions form a glassy state at 77 K over a wide concentration of ILs. They have potential as novel cryopreservation/refolding solvents for proteins. However, even if proteins in glass-forming concentrations of ILs are preserved at 77 K, the recovery of activity and the structure of the proteins after cryopreservation are still unclear. To achieve high recovery of ...
Direct electron transfer between cytochrome c and nanostar-coated pyrolytic graphite electrodes was observed with the protein in solution. The electrochemical response was improved at nanostars functionalized with a 1 : 1 mixture of 11-mercaptoundecanoic acid and 4-mercaptobenzoic acid in comparison with gold nanospheres coated with a similar ...