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Updated: Nov 6, 2025

Electrochemical Detection of Deuterium Kinetic Isotope Effect on Extracellular Electron Transport in Shewanella oneidensis MR-1
Published on: April 16, 2018
Erv1 and Cytochrome c Mediate Rapid Electron Transfer via A Collision-Type Interaction
Esra Peker1, Alican J Erdogan1, Alexander N Volkov2
1Institute for Biochemistry, Redox Biochemistry, University of Cologne, Zuelpicher Str. 47a, 50674 Cologne, Germany.
Mitochondrial electron transfer between Erv1 and cytochrome c (Cc) occurs via transient collisions, not stable complexes. This interaction protects against reactive oxygen species.
Area of Science:
- Biochemistry
- Mitochondrial Biology
- Protein Interactions
Background:
- The mitochondrial disulfide relay is crucial for oxidative protein folding.
- This process depends on electron transfer (ET) from Erv1 to cytochrome c (Cc).
Purpose of the Study:
- To investigate the interaction mechanism between yeast cytochrome c and Erv1.
- To understand how this interaction facilitates electron transfer without stable complex formation.
Main Methods:
- Solution NMR spectroscopy was used to study the yeast Cc-Erv1 system.
- Molecular modeling was employed to rationalize the observed transient interactions.
Main Results:
- The yeast Cc-Erv1 system is functionally active.
- No stable, observable binding between Cc and Erv1 was detected.
- A collision-type mechanism facilitates fast ET from Erv1 to Cc over a large surface area.
Conclusions:
- Mitochondrial electron transfer between Cc and Erv1 occurs through transient, collision-based interactions.
- This mechanism avoids canonical protein complex formation.
- The interaction likely prevents direct ET to molecular oxygen, offering protection against reactive oxygen species.
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