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Electron-transfer processes of cytochrome C at interfaces. New insights by surface-enhanced resonance Raman spectroscopy.

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TLDR
It is shown that physiologically relevant electric field strengths can effectively modulate the electron-transfer dynamics and induce conformational transitions in heme protein cytochrome c.
Abstract
The heme protein cytochrome c acts as an electron carrier at the mitochondrial-membrane interface and thus exerts its function under the influence of strong electric fields. To assess possible consequences of electric fields on the redox processes of cytochrome c, the protein can be immobilized to self-assembled monolayers on electrodes and studied by surface-enhanced resonance Raman spectroscopy. Such model systems may mimic some essential features of biological interfaces including local electric field strengths. It is shown that physiologically relevant electric field strengths can effectively modulate the electron-transfer dynamics and induce conformational transitions.

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Citations
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Journal ArticleDOI

A review on the fabrication of substrates for surface enhanced Raman spectroscopy and their applications in analytical chemistry.

TL;DR: This review shows that highly enhancing SERS substrates with a high degree of reliability and reproducibility can now be fabricated at relative low cost, indicating that SERS may finally realize its full potential as a very sensitive tool for routine analytical applications.
Journal ArticleDOI

Using Raman spectroscopy to characterize biological materials

TL;DR: A robust approach for sample preparation, instrumentation, acquisition parameters and data processing is explored and it is expected that a typical Raman experiment can be performed by a nonspecialist user to generate high-quality data for biological materials analysis.
Journal ArticleDOI

Direct Electrochemistry of Redox Enzymes as a Tool for Mechanistic Studies

TL;DR: This review regards the use of dynamic electrochemistry to study the mechanism of redox enzymes, with exclusive emphasis on the configuration where the protein is adsorbed onto an electrode and electron tranfer is direct.
Journal ArticleDOI

Oriented electric fields as future smart reagents in chemistry

TL;DR: It is postulate that, as experimental techniques mature, chemical syntheses may become an exercise in zapping oriented molecules with OEEFs, and the wide-ranging potential of using OEEF to catalyse and control a variety of non-redox reactions and impart selectivity at will is discussed.
Journal ArticleDOI

Surface-enhanced Raman scattering for protein detection

TL;DR: This review outlines the development of SERS-based methods for proteins with particular focus on the proposed protein-mediated Sers-active substrates and their applications in label-free and Raman dye-labeled protein detection.
References
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Journal ArticleDOI

The asymmetric distribution of charges on the surface of horse cytochrome c. Functional implications.

TL;DR: This model describes quantitatively the relative activities of those CDNP-lysine cytochromes c which are modified outside of the interaction domain and it allows correction of the activities of Those modified inside the domain, on the front surface of the molecule, for the change in dipole moment.
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Theory of the interfacial potential distribution and reversible voltammetric response of electrodes coated with electroactive molecular films.

TL;DR: The driving force for reversible electron transfer between the metal and electroactive adsorbate is calculated from the interfacial potential distribution and is used to predict the current-voltage wave shape in cyclic voltammetric experiments.
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An electrochemical approach to investigate gated electron transfer using a physiological model system: Cytochrome c immobilized on carboxylic acid-terminated alkanethiol self-assembled monolayers on gold electrodes

TL;DR: In this article, the effects of alkanethiol chain length, ionic strength, pH, and viscosity of supporting electrolyte on the ET kinetics were studied, and it was shown that the ET rates through long ALK chains were slow because electron tunneling through th...
Journal ArticleDOI

Spectroscopic Characterization of Nonnative Conformational States of Cytochrome c

TL;DR: In this paper, a global spectral analysis of all species that differ with respect to the heme structure were identified and characterized in terms of the spin and ligation state of the Heme as well as of protein secondary and tertiary structure changes.
Journal ArticleDOI

Proton-coupled electron transfer of cytochrome c.

TL;DR: It is concluded that at the Ag/SAM interface the energy barrier for the PT processes of the adsorbed Cyt-c is raised by the electric field, which may represent a possible mechanism for controlling biological redox reactions via changes of the transmembrane potential.
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