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Updated: Jun 24, 2026

Imaging Plasma Membrane Deformations With pTIRFM

Imaging Plasma Membrane Deformations With pTIRFM

Published on: April 2, 2014

Proton-coupled electron transfer of cytochrome c.

D H Murgida¹, P Hildebrandt

¹Contribution from the Max-Planck-Institut für Strahlenchemie, Stiftstrasse 34-36, D-45470 Mülheim, Germany.

Journal of the American Chemical Society

|July 18, 2001

Summary

This summary is machine-generated.

This study investigated electron transfer in cytochrome c (Cyt-c) adsorbed on electrodes. Researchers found that electric fields at the interface influence proton transfer, potentially controlling biological redox reactions.

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Area of Science:

Electrochemistry
Biophysical Chemistry
Surface Science

Background:

Cytochrome c (Cyt-c) is a crucial heme protein involved in electron transfer (ET).
Understanding ET dynamics at interfaces is vital for bioelectronic applications.
Self-assembled monolayers (SAMs) provide a platform to control protein adsorption and ET.

Purpose of the Study:

To investigate the distance dependence of electron transfer in adsorbed Cyt-c.
To explore the role of proton transfer (PT) in the redox dynamics of adsorbed Cyt-c.
To elucidate the influence of the electrode interface electric field on Cyt-c redox reactions.

Main Methods:

Electrostatic binding of Cyt-c to omega-carboxyl alkanethiol SAMs on Ag electrodes.
Time-resolved surface-enhanced resonance Raman (SERR) spectroscopy to monitor ET dynamics.
Analysis of ET rate constants and kinetic H/D effects across varying SAM chain lengths.

Main Results:

ET rate constants showed an exponential distance dependence for longer SAM chains (C16, C11).
A transition to nonexponential distance dependence was observed for shorter chains (C6, C3, C2).
A significant kinetic H/D isotope effect indicated coupled proton transfer, increasing with shorter chain lengths.

Conclusions:

The electric field at the Ag/SAM interface enhances the energy barrier for PT in adsorbed Cyt-c.
This effect increases with proximity to the electrode, potentially making nuclear tunneling rate-limiting.
The electric field-modulated proton-coupled ET mechanism offers a pathway for controlling biological redox reactions, analogous to transmembrane potential effects.