Electric-field effects on the interfacial electron transfer and protein dynamics of cytochrome c

Time-resolved surface enhanced resonance Raman and surface enhanced infrared absorption spectroscopy have been employed to study the interfacial redox process of cytochrome c (Cyt-c) immobilised on various metal electrodes coated with self-assembled monolayers (SAMs) of carboxyl-terminated mercaptan...

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Detalles Bibliográficos
Autores principales: Khoa Ly, H., Wisitruangsakul, N., Sezer, M., Feng, J.-J., Kranich, A., Weidinger, I.M., Zebger, I., Murgida, D.H., Hildebrandt, P.
Formato: JOUR
Materias:
Cytochrome c
Electric field
Electron transfer
Surface enhanced infrared spectroscopy
Surface enhanced Raman spectroscopy
Dynamics
Electric fields
Electrodes
Electron transitions
Electron tunneling
Gold
Hydrogen bonds
Infrared spectroscopy
Isotopes
Proteins
Raman spectroscopy
Self assembled monolayers
Cytochrome C
Electric field strength
Heterogeneous electron transfer
High electric fields
Hydrogen bond networks
Interfacial electron transfer
Kinetic isotope effects
Metal electrodes
Methylene groups
Protein dynamics
Rate limiting
Rate-limiting steps
Re-orientation
Redox process
Sams
Structural change
Surface enhanced infrared absorption spectroscopy
Surface enhanced resonance
Time-resolved
Zero charge
Electric field effects
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_15726657_v660_n2_p367_KhoaLy
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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