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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Detalles Bibliográficos
Autores principales:	Alvarez-Paggi, D., Martín, D.F., Debiase, P.M., Hildebrandt, P., Martí, M.A., Murgida, D.H.
Formato:	JOUR
Materias:	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 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 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
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_00027863_v132_n16_p5769_AlvarezPaggi
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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