Molecular basis of coupled protein and electron transfer dynamics of cytochrome c in biomimetic complexes
Direct electron transfer (ET) of redox proteins immobilized on biomimetic or biocompatible electrodes represents an active field of fundamental and applied research. In this context, several groups have reported for a variety of proteins unexpected distance dependencies of the ET rate, whose origin...
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2010
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00027863_v132_n16_p5769_AlvarezPaggi http://hdl.handle.net/20.500.12110/paper_00027863_v132_n16_p5769_AlvarezPaggi |
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paper:paper_00027863_v132_n16_p5769_AlvarezPaggi2023-06-08T14:22:46Z Molecular basis of coupled protein and electron transfer dynamics of cytochrome c in biomimetic complexes Active field Alkylthiols Applied research Binding configuration Biomimetic complex Concomitant binding Cytochrome C Direct electron transfer Electrochemical data Electron transfer dynamics Electronic coupling Energy calculation Low-amplitude Lysine residues MD simulation Molecular basis Molecular descriptions Molecular dynamics simulations Optimum coupling Pathway analysis Protein dynamics Protein orientation Redox proteins Thermal fluctuations Tunneling probabilities Amino acids Binding energy Biomimetics Dynamics Electric dipole moments Electron transitions Molecular dynamics Monolayers Proteins carboxy terminated alkylthiol cytochrome c gold lysine protein self assembled monolayer thiol derivative unclassified drug biomimetic material cytochrome c immobilized enzyme amplitude modulation article binding affinity biomimetics calculation carboxy terminal sequence complex formation controlled study cross coupling reaction dipole electric field electricity electrode electron electron transport energy material coating molecular dynamics oxidation protein analysis protein stability thermodynamics tuning curve chemistry electrochemistry electron transport enzyme specificity protein tertiary structure static electricity Biomimetic Materials Cytochromes c Electrochemistry Electron Transport Enzymes, Immobilized Gold Molecular Dynamics Simulation Protein Structure, Tertiary Static Electricity Substrate Specificity Sulfhydryl Compounds Thermodynamics Direct electron transfer (ET) of redox proteins immobilized on biomimetic or biocompatible electrodes represents an active field of fundamental and applied research. In this context, several groups have reported for a variety of proteins unexpected distance dependencies of the ET rate, whose origin remains largely speculative and controversial, but appears to be a quite general phenomenon. Here we have employed molecular dynamics (MD) simulations and electron pathway analyses to study the ET properties of cytochrome c (Cyt) electrostatically immobilized on Au coated by carboxyl-terminated alkylthiols. The MD simulations and concomitant binding energy calculations allow identification of preferred binding configurations of the oxidized and reduced Cyt which are established via different lysine residues and, thus, correspond to different orientations and dipole moments. Calculations of the electronic coupling matrices for the various Cyt/self-assembled monolayer (SAM) complexes indicate that the thermodynamically preferred protein orientations do not coincide with the orientations of optimum coupling. These findings demonstrate that the ET of the immobilized Cyt is controlled by an interplay between protein dynamics and tunneling probabilities. Protein dynamics exerts two level of tuning on the electronic coupling via reorientation (coarse) and low amplitude thermal fluctuations (fine). Upon operating the Au support as an electrode, electric-field-dependent alignment of the protein dipole moment becomes an additional determinant for the protein dynamics and thus for the overall ET rate. The present results provide a consistent molecular description of previous (spectro)electrochemical data and allow conclusions concerning the coupling of protein dynamics and ET of Cyt in physiological complexes. © 2010 American Chemical Society. 2010 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00027863_v132_n16_p5769_AlvarezPaggi http://hdl.handle.net/20.500.12110/paper_00027863_v132_n16_p5769_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 |
Active field Alkylthiols Applied research Binding configuration Biomimetic complex Concomitant binding Cytochrome C Direct electron transfer Electrochemical data Electron transfer dynamics Electronic coupling Energy calculation Low-amplitude Lysine residues MD simulation Molecular basis Molecular descriptions Molecular dynamics simulations Optimum coupling Pathway analysis Protein dynamics Protein orientation Redox proteins Thermal fluctuations Tunneling probabilities Amino acids Binding energy Biomimetics Dynamics Electric dipole moments Electron transitions Molecular dynamics Monolayers Proteins carboxy terminated alkylthiol cytochrome c gold lysine protein self assembled monolayer thiol derivative unclassified drug biomimetic material cytochrome c immobilized enzyme amplitude modulation article binding affinity biomimetics calculation carboxy terminal sequence complex formation controlled study cross coupling reaction dipole electric field electricity electrode electron electron transport energy material coating molecular dynamics oxidation protein analysis protein stability thermodynamics tuning curve chemistry electrochemistry electron transport enzyme specificity protein tertiary structure static electricity Biomimetic Materials Cytochromes c Electrochemistry Electron Transport Enzymes, Immobilized Gold Molecular Dynamics Simulation Protein Structure, Tertiary Static Electricity Substrate Specificity Sulfhydryl Compounds Thermodynamics |
| spellingShingle |
Active field Alkylthiols Applied research Binding configuration Biomimetic complex Concomitant binding Cytochrome C Direct electron transfer Electrochemical data Electron transfer dynamics Electronic coupling Energy calculation Low-amplitude Lysine residues MD simulation Molecular basis Molecular descriptions Molecular dynamics simulations Optimum coupling Pathway analysis Protein dynamics Protein orientation Redox proteins Thermal fluctuations Tunneling probabilities Amino acids Binding energy Biomimetics Dynamics Electric dipole moments Electron transitions Molecular dynamics Monolayers Proteins carboxy terminated alkylthiol cytochrome c gold lysine protein self assembled monolayer thiol derivative unclassified drug biomimetic material cytochrome c immobilized enzyme amplitude modulation article binding affinity biomimetics calculation carboxy terminal sequence complex formation controlled study cross coupling reaction dipole electric field electricity electrode electron electron transport energy material coating molecular dynamics oxidation protein analysis protein stability thermodynamics tuning curve chemistry electrochemistry electron transport enzyme specificity protein tertiary structure static electricity Biomimetic Materials Cytochromes c Electrochemistry Electron Transport Enzymes, Immobilized Gold Molecular Dynamics Simulation Protein Structure, Tertiary Static Electricity Substrate Specificity Sulfhydryl Compounds Thermodynamics Molecular basis of coupled protein and electron transfer dynamics of cytochrome c in biomimetic complexes |
| topic_facet |
Active field Alkylthiols Applied research Binding configuration Biomimetic complex Concomitant binding Cytochrome C Direct electron transfer Electrochemical data Electron transfer dynamics Electronic coupling Energy calculation Low-amplitude Lysine residues MD simulation Molecular basis Molecular descriptions Molecular dynamics simulations Optimum coupling Pathway analysis Protein dynamics Protein orientation Redox proteins Thermal fluctuations Tunneling probabilities Amino acids Binding energy Biomimetics Dynamics Electric dipole moments Electron transitions Molecular dynamics Monolayers Proteins carboxy terminated alkylthiol cytochrome c gold lysine protein self assembled monolayer thiol derivative unclassified drug biomimetic material cytochrome c immobilized enzyme amplitude modulation article binding affinity biomimetics calculation carboxy terminal sequence complex formation controlled study cross coupling reaction dipole electric field electricity electrode electron electron transport energy material coating molecular dynamics oxidation protein analysis protein stability thermodynamics tuning curve chemistry electrochemistry electron transport enzyme specificity protein tertiary structure static electricity Biomimetic Materials Cytochromes c Electrochemistry Electron Transport Enzymes, Immobilized Gold Molecular Dynamics Simulation Protein Structure, Tertiary Static Electricity Substrate Specificity Sulfhydryl Compounds Thermodynamics |
| description |
Direct electron transfer (ET) of redox proteins immobilized on biomimetic or biocompatible electrodes represents an active field of fundamental and applied research. In this context, several groups have reported for a variety of proteins unexpected distance dependencies of the ET rate, whose origin remains largely speculative and controversial, but appears to be a quite general phenomenon. Here we have employed molecular dynamics (MD) simulations and electron pathway analyses to study the ET properties of cytochrome c (Cyt) electrostatically immobilized on Au coated by carboxyl-terminated alkylthiols. The MD simulations and concomitant binding energy calculations allow identification of preferred binding configurations of the oxidized and reduced Cyt which are established via different lysine residues and, thus, correspond to different orientations and dipole moments. Calculations of the electronic coupling matrices for the various Cyt/self-assembled monolayer (SAM) complexes indicate that the thermodynamically preferred protein orientations do not coincide with the orientations of optimum coupling. These findings demonstrate that the ET of the immobilized Cyt is controlled by an interplay between protein dynamics and tunneling probabilities. Protein dynamics exerts two level of tuning on the electronic coupling via reorientation (coarse) and low amplitude thermal fluctuations (fine). Upon operating the Au support as an electrode, electric-field-dependent alignment of the protein dipole moment becomes an additional determinant for the protein dynamics and thus for the overall ET rate. The present results provide a consistent molecular description of previous (spectro)electrochemical data and allow conclusions concerning the coupling of protein dynamics and ET of Cyt in physiological complexes. © 2010 American Chemical Society. |
| title |
Molecular basis of coupled protein and electron transfer dynamics of cytochrome c in biomimetic complexes |
| title_short |
Molecular basis of coupled protein and electron transfer dynamics of cytochrome c in biomimetic complexes |
| title_full |
Molecular basis of coupled protein and electron transfer dynamics of cytochrome c in biomimetic complexes |
| title_fullStr |
Molecular basis of coupled protein and electron transfer dynamics of cytochrome c in biomimetic complexes |
| title_full_unstemmed |
Molecular basis of coupled protein and electron transfer dynamics of cytochrome c in biomimetic complexes |
| title_sort |
molecular basis of coupled protein and electron transfer dynamics of cytochrome c in biomimetic complexes |
| publishDate |
2010 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00027863_v132_n16_p5769_AlvarezPaggi http://hdl.handle.net/20.500.12110/paper_00027863_v132_n16_p5769_AlvarezPaggi |
| _version_ |
1768542575713583104 |