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A High-Potential Redox Landscape Bump Enhances Electron Bifurcation Efficiency
Emily Y Wang1, Andrew J Smith1, David N Beratan1,2,3
1Department of Chemistry, Duke University, Durham, North Carolina27708, United States.
The Journal of Physical Chemistry. B
|July 23, 2026
Summary
Electron bifurcation (EB) uses a redox potential bump in enzymes like NfnI to boost efficiency by preventing electron short-circuiting. This structural feature enhances biological energy transduction but can reduce electron flow.
Area of Science:
- Biochemistry
- Bioenergetics
- Protein Engineering
Background:
- Electron bifurcation (EB) is a key biological process for energy transduction and catalysis.
- EB enzymes separate electron pairs for efficient energy transfer.
- The NADH-dependent ferredoxin-NADP+ oxidoreductase I (NfnI) enzyme features a high-potential iron-sulfur cluster (H1).
Purpose of the Study:
- To investigate the role of the H1 cofactor's redox potential bump in NfnI's energy transduction.
- To model the impact of this structural feature on electron flow and EB efficiency.
Main Methods:
- Utilized a fully correlated, three-reservoir master equation approach.
- Modeled multielectron flux within the NfnI enzyme.
Main Results:
- The H1 cofactor's reduction potential bump significantly enhances EB efficiency.
- This enhancement occurs by suppressing energy-dissipating electron short-circuiting via the occupancy effect.
- Increased EB efficiency comes at the cost of reduced EB flux.
Conclusions:
- The H1 cofactor's redox landscape is crucial for optimizing EB efficiency in NfnI.
- Findings reveal a structure-function principle in natural EB proteins.
- Provides insights for designing novel proteins with controlled charge flow.
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