ArticleProceedings of the National Academy of Sciences of the United States of America2022
An uncharacteristically low-potential flavin governs the energy landscape of electron bifurcation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed.
- pK Values of the Cofactor Tune the Redox Regime of Flavoenzymes.Life (Basel, Switzerland) · 2026Article
- Photoinduced Electron Transfer Informs on Pathway Coupling in Flavin-Based Electron Bifurcation.ACS bio & med chem Au · 2026Article
- Design of Light Driven Hole Bifurcating Proteins.ACS central science · 2025Article
- Identification of electron transfer enzymes inJournal of bacteriology · 2025Article
- Evolutionary obstacles and not C-F bond strength make PFAS persistent.Microbial biotechnology · 2024Article
- Rapid-reaction kinetics of the bifurcating NADThe Journal of biological chemistry · 2023Article
- Machine Learning for Efficient Prediction of Protein Redox Potential: The Flavoproteins Case.Journal of chemical information and modeling · 2022Article
- Site-Differentiated Iron-Sulfur Cluster Ligation Affects Flavin-Based Electron Bifurcation Activity.Metabolites · 2022Article
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7 authors.
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Abstract
Electron bifurcation, an energy-conserving process utilized extensively throughout all domains of life, represents an elegant means of generating high-energy products from substrates with less reducing potential. The coordinated coupling of exergonic and endergonic reactions has been shown to operate over an electrochemical potential of ∼1.3 V through the activity of a unique flavin cofactor in the enzyme NADH-dependent ferredoxin-NADP+ oxidoreductase I. The inferred energy landscape has features unprecedented in biochemistry and presents novel energetic challenges, the most intriguing being a large thermodynamically uphill step for the first electron transfer of the bifurcation reaction. However, ambiguities in the energy landscape at the bifurcating site deriving from overlapping flavin spectral signatures have impeded a comprehensive understanding of the specific mechanistic contributions afforded by thermodynamic and kinetic factors. Here, we elucidate an uncharacteristically low two-electron potential of the bifurcating flavin, resolving the energetic challenge of the first bifurcation event.
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