ArticleNature communications2019
Low potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors.
Article in Nature communications, 2019. 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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Who cites it
8 citing papers in PubMed, 27 citations in OpenAlex.
- Breaking aromaticity in the anaerobic degradation pathway of phenanthrene comprises only ATP-independent type III aryl-CoA reductases.Communications biology · 2026Article
- The ATP-independent dihydro-2-phenanthroyl-CoA reductase AprC catalyzes two consecutive two-electron reduction steps of dihydro-2-phenanthroyl-CoA to hexahydro-2-phenanthroyl-CoA in anaerobic phenanthrene degradation.Applied and environmental microbiology · 2026Article
- Characterization of 2-phenanthroyl-CoA reductase, an ATP-independent type III aryl-CoA reductase involved in anaerobic phenanthrene degradation.Applied and environmental microbiology · 2025Article
- Anaerobic degradation of polycyclic aromatic hydrocarbons.Applied and environmental microbiology · 2025Review
- Parkinsonism-Associated Protein DJ-1 Is an Antagonist, Not an Eraser, for Protein Glycation.Biochemistry · 2023Article
- Biocatalytic Reduction Reactions from a Chemist's Perspective.Angewandte Chemie (International ed. in English) · 2021Review
- Spectroscopic evidence for direct flavin-flavin contact in a bifurcating electron transfer flavoprotein.The Journal of biological chemistry · 2020Article
- A recently evolved diflavin-containing monomeric nitrate reductase is responsible for highly efficient bacterial nitrate assimilation.The Journal of biological chemistry · 2020Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
Abstract
Hydride transfers play a crucial role in a multitude of biological redox reactions and are mediated by flavin, deazaflavin or nicotinamide adenine dinucleotide cofactors at standard redox potentials ranging from 0 to -340 mV. 2-Naphthoyl-CoA reductase, a key enzyme of oxygen-independent bacterial naphthalene degradation, uses a low-potential one-electron donor for the two-electron dearomatization of its substrate below the redox limit of known biological hydride transfer processes at E°' = -493 mV. Here we demonstrate by X-ray structural analyses, QM/MM computational studies, and multiple spectroscopy/activity based titrations that highly cooperative electron transfer (n = 3) from a low-potential one-electron (FAD) to a two-electron (FMN) transferring flavin cofactor is the key to overcome the resonance stabilized aromatic system by hydride transfer in a highly hydrophobic pocket. The results evidence how the protein environment inversely functionalizes two flavins to switch from low-potential one-electron to hydride transfer at the thermodynamic limit of flavin redox chemistry.
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Registered trials
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