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Flavins in the electron bifurcation process

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Molecular basis of the flavin‐based electron‐bifurcating caffeyl‐CoA reductase reaction
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Redox bifurcations: Mechanisms and importance to life now, and at its origin
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A two [4Fe-4S]-cluster-containing ferredoxin as an alternative electron donor for 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans
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Energetics of the one-electron reduction steps of riboflavin, FMN and FAD to their fully reduced forms
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The protonmotive Q cycle: A general formulation
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Energy conservation via electron bifurcating ferredoxin reduction and proton/Na+ translocating ferredoxin oxidation
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The mechanism of ubihydroquinone oxidation at the Qo-site of the cytochrome bc1 complex
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The multitude of iron–sulfur clusters in respiratory complex I
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Electron bifurcation
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Energy in Ancient Metabolism
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Hydrogen, metals, bifurcating electrons, and proton gradients: The early evolution of biological energy conservation
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Sweating the assets of flavin cofactors: new insight of chemical versatility from knowledge of structure and mechanism
inferredcites →https://doi.org/10.1016/s0021-9258(18)91859-4openalex-snapshot
Oxidation-Reduction Properties of Flavodoxin from Peptostreptococcus elsdenii
inferredcites →https://doi.org/10.1016/s0167-4838(99)00139-9openalex-snapshot
The functions of the flavin contact residues, αArg249 and βTyr16, in human electron transfer flavoprotein
inferredcites →https://doi.org/10.1021/acs.accounts.7b00327openalex-snapshot
Electron Bifurcation: Thermodynamics and Kinetics of Two-Electron Brokering in Biological Redox Chemistry
inferredcites →https://doi.org/10.1021/acs.biochem.7b00389openalex-snapshot
The Electron Bifurcating FixABCX Protein Complex from Azotobacter vinelandii: Generation of Low-Potential Reducing Equivalents for Nitrogenase Catalysis
inferredcites →https://doi.org/10.1021/acs.chemrev.7b00650openalex-snapshot
Same Substrate, Many Reactions: Oxygen Activation in Flavoenzymes
inferredcites →https://doi.org/10.1021/bi00007a009openalex-snapshot
Three-Dimensional Structure of Butyryl-CoA Dehydrogenase from Megasphaera elsdenii
inferredcites →https://doi.org/10.1021/bi00199a034openalex-snapshot
Thermodynamic Analysis of Flavin in Mitochondrial NADH:Ubiquinone Oxidoreductase (Complex I)
inferredcites →https://doi.org/10.1021/bi036179iopenalex-snapshot
Thermodynamic Basis of Electron Transfer in Dihydroorotate Dehydrogenase B from Lactococcus lactis: Analysis by Potentiometry, EPR Spectroscopy, and ENDOR Spectroscopy
inferredcites →https://doi.org/10.1021/bi0616293openalex-snapshot
Modulation of the Redox Properties of the Flavin Cofactor through Hydrogen-Bonding Interactions with the N(5) Atom: Role of αSer254 in the Electron-Transfer Flavoprotein from the Methylotrophic Bacterium W3A1
inferredcites →https://doi.org/10.1021/bi962124nopenalex-snapshot
The Cumulative Electrostatic Effect of Aromatic Stacking Interactions and the Negative Electrostatic Environment of the Flavin Mononucleotide Binding Site Is a Major Determinant of the Reduction Potential for the Flavodoxin from Desulfovibrio vulgaris [Hildenborough]
inferredcites →https://doi.org/10.1021/bi962180oopenalex-snapshot
Control of Oxidation−Reduction Potentials in Flavodoxin from Clostridium beijerinckii: The Role of Conformation Changes,
inferredcites →https://doi.org/10.1021/bi991172fopenalex-snapshot
Role of Glutamate-59 Hydrogen Bonded to N(3)H of the Flavin Mononucleotide Cofactor in the Modulation of the Redox Potentials of theClostridium beijerinckiiFlavodoxin. Glutamate-59 Is Not Responsible for the pH Dependency but Contributes to the Stabilization of the Flavin Semiquinone
inferredcites →https://doi.org/10.1021/ja806540jopenalex-snapshot
What Makes the Difference between a Cryptochrome and DNA Photolyase? A Spectroelectrochemical Comparison of the Flavin Redox Transitions
inferredcites →https://doi.org/10.1023/b:jobb.0000019599.43969.33openalex-snapshot
Energy-Converting [NiFe] Hydrogenases from Archaea and Extremophiles: Ancestors of Complex I
inferredcites →https://doi.org/10.1023/b:pres.0000036884.57303.2eopenalex-snapshot
Structural Aspects of Plant Ferredoxin : NADP+ Oxidoreductases
inferredcites →https://doi.org/10.1038/352172a0openalex-snapshot
Convergent evolution of similar function in two structurally divergent enzymes
inferredcites →https://doi.org/10.1038/355796a0openalex-snapshot
Nature of biological electron transfer
inferredcites →https://doi.org/10.1038/nchembio.2348openalex-snapshot
Mechanistic insights into energy conservation by flavin-based electron bifurcation
inferredcites →https://doi.org/10.1038/nrmicro1931openalex-snapshot
Methanogenic archaea: ecologically relevant differences in energy conservation
inferredcites →https://doi.org/10.1038/s41467-017-01746-3openalex-snapshot
The semiquinone swing in the bifurcating electron transferring flavoprotein/butyryl-CoA dehydrogenase complex from Clostridium difficile
inferredcites →https://doi.org/10.1038/s41467-019-10078-3openalex-snapshot
Low potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors
inferredcites →https://doi.org/10.1038/s41467-019-10429-0openalex-snapshot
A mechanism to prevent production of reactive oxygen species by Escherichia coli respiratory complex I
inferredcites →https://doi.org/10.1039/c2np20069dopenalex-snapshot
Flavoenzymes: Versatile catalysts in biosynthetic pathways
inferredcites →https://doi.org/10.1046/j.1432-1033.2003.03450.xopenalex-snapshot
Acryloyl‐CoA reductase from Clostridium propionicum
inferredcites →https://doi.org/10.1046/j.1432-1327.1999.00767.xopenalex-snapshot
The effects of pH and semiquinone formation on the oxidation–reduction potentials of flavin mononucleotide
inferredcites →https://doi.org/10.1073/pnas.1003653107openalex-snapshot
Protein complexing in a methanogen suggests electron bifurcation and electron delivery from formate to heterodisulfide reductase
inferredcites →https://doi.org/10.1073/pnas.1016761108openalex-snapshot
Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in hydrogenotrophic methanogenic archaea
inferredcites →https://doi.org/10.1073/pnas.1819636116openalex-snapshot
One-megadalton metalloenzyme complex in Geobacter metallireducens involved in benzene ring reduction beyond the biological redox window
inferredcites →https://doi.org/10.1073/pnas.1908578116openalex-snapshot
Structure and function of an unusual flavodoxin from the domain Archaea
inferredcites →https://doi.org/10.1073/pnas.2010815117openalex-snapshot
Universal free-energy landscape produces efficient and reversible electron bifurcation
inferredcites →https://doi.org/10.1073/pnas.69.11.3185openalex-snapshot
Structure of the Oxidized Form of a Flavodoxin at 2.5-Å Resolution: Resolution of the Phase Ambiguity by Anomalous Scattering
inferredcites →https://doi.org/10.1073/pnas.93.25.14355openalex-snapshot
Three-dimensional structure of human electron transfer flavoprotein to 2.1-Å resolution
inferredcites →https://doi.org/10.1074/jbc.m010853200openalex-snapshot
αArg-237 in Methylophilus methylotrophus (sp. W3A1) Electron-transferring Flavoprotein Affords ∼200-Millivolt Stabilization of the FAD Anionic Semiquinone and a Kinetic Block on Full Reduction to the Dihydroquinone
inferredcites →https://doi.org/10.1074/jbc.m112.395038openalex-snapshot
A Bacterial Electron-bifurcating Hydrogenase
inferredcites →https://doi.org/10.1074/jbc.m112.444919openalex-snapshot
An Electron-bifurcating Caffeyl-CoA Reductase
inferredcites →https://doi.org/10.1074/jbc.m113.521013openalex-snapshot
Studies on the Mechanism of Electron Bifurcation Catalyzed by Electron Transferring Flavoprotein (Etf) and Butyryl-CoA Dehydrogenase (Bcd) of Acidaminococcus fermentans
inferredcites →https://doi.org/10.1074/jbc.m115.656520openalex-snapshot
Insights into Flavin-based Electron Bifurcation via the NADH-dependent Reduced Ferredoxin:NADP Oxidoreductase Structure
inferredcites →https://doi.org/10.1074/jbc.m116.726299openalex-snapshot
Reduction of Flavodoxin by Electron Bifurcation and Sodium Ion-dependent Reoxidation by NAD+ Catalyzed by Ferredoxin-NAD+ Reductase (Rnf)
inferredcites →https://doi.org/10.1074/jbc.m117.794172openalex-snapshot
Two functionally distinct NADP+-dependent ferredoxin oxidoreductases maintain the primary redox balance of Pyrococcus furiosus
inferredcites →https://doi.org/10.1074/jbc.m117.794214openalex-snapshot
Equilibrium and ultrafast kinetic studies manipulating electron transfer: A short-lived flavin semiquinone is not sufficient for electron bifurcation
inferredcites →https://doi.org/10.1074/jbc.ra117.000707openalex-snapshot
Distinct properties underlie flavin-based electron bifurcation in a novel electron transfer flavoprotein FixAB from Rhodopseudomonas palustris
inferredcites →https://doi.org/10.1074/jbc.ra118.005653openalex-snapshot
The catalytic mechanism of electron-bifurcating electron transfer flavoproteins (ETFs) involves an intermediary complex with NAD+
inferredcites →https://doi.org/10.1074/jbc.ra120.016017openalex-snapshot
Rapid kinetics reveal surprising flavin chemistry in bifurcating electron transfer flavoprotein from Acidaminococcus fermentans
inferredcites →https://doi.org/10.1093/emboj/20.4.650openalex-snapshot
Crystal structure of dihydropyrimidine dehydrogenase, a major determinant of the pharmacokinetics of the anti‐cancer drug 5‐fluorouracil
inferredcites →https://doi.org/10.1093/jb/mvt026openalex-snapshot
Interaction between NADH and electron-transferring flavoprotein from Megasphaera elsdenii
inferredcites →https://doi.org/10.1096/fasebj.9.9.7601336openalex-snapshot
Structure and mechanism of action of the Acyl‐CoA dehydrogenases 1
inferredcites →https://doi.org/10.1111/1462-2920.12493openalex-snapshot
A novel mode of lactate metabolism in strictly anaerobic bacteria
inferredcites →https://doi.org/10.1111/1462-2920.12689openalex-snapshot
The FlxABCD ‐ HdrABC proteins correspond to a novel NADH dehydrogenase/heterodisulfide reductase widespread in anaerobic bacteria and involved in ethanol metabolism in D esulfovibrio vulgaris H ildenborough
inferredcites →https://doi.org/10.1111/1462-2920.14899openalex-snapshot
DsrL mediates electron transfer between NADH and rDsrAB in Allochromatium vinosum
inferredcites →https://doi.org/10.1111/febs.13308openalex-snapshot
Reduction of ferredoxin or oxygen by flavin‐based electron bifurcation in Megasphaera elsdenii
inferredcites →https://doi.org/10.1111/febs.15343openalex-snapshot
Modulations of the reduction potentials of flavin‐based electron bifurcation complexes and semiquinone stabilities are key to control directional electron flow
inferredcites →https://doi.org/10.1111/febs.15505openalex-snapshot
Structural and spectroscopic characterization of a HdrA‐like subunit from Hyphomicrobium denitrificans
inferredcites →https://doi.org/10.1111/j.1432-1033.1990.tb19331.xopenalex-snapshot
Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum (strain Marburg)
inferredcites →https://doi.org/10.1111/j.1432-1033.1994.tb18608.xopenalex-snapshot
H2: heterodisulfide oxidoreductase complex from Methanobacterium thermoautotrophicum
inferredcites →https://doi.org/10.1111/j.1432-1033.1996.0662u.xopenalex-snapshot
Analysis of the Oxidation‐Reduction Potentials of Recombinant Ferredoxin‐NADP + Reductase from Spinach Chloroplasts
inferredcites →https://doi.org/10.1111/j.1432-1033.1997.00393.xopenalex-snapshot
Regulation of the Flavin Redox Potential by Flavin‐Binding Antibodies
inferredcites →https://doi.org/10.1111/j.1742-4658.2007.06107.xopenalex-snapshot
Dynamics driving function − new insights from electron transferring flavoproteins and partner complexes
inferredcites →https://doi.org/10.1111/mmi.12238openalex-snapshot
Identification and characterization of 2‐naphthoyl‐coenzyme A reductase, the prototype of a novel class of dearomatizing reductases
inferredcites →https://doi.org/10.1126/sciadv.aaw9059openalex-snapshot
Life on the thermodynamic edge: Respiratory growth of an acetotrophic methanogen
inferredcites →https://doi.org/10.1126/science.1986412openalex-snapshot
Atomic Structure of Ferredoxin-NADP + Reductase: Prototype for a Structurally Novel Flavoenzyme Family
inferredcites →https://doi.org/10.1126/science.aaf9284openalex-snapshot
The methanogenic CO 2 reducing-and-fixing enzyme is bifunctional and contains 46 [4Fe-4S] clusters
inferredcites →https://doi.org/10.1126/science.aan0425openalex-snapshot
Methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction
inferredcites →https://doi.org/10.1128/jb.00321-13openalex-snapshot
Effect of an Oxygen-Tolerant Bifurcating Butyryl Coenzyme A Dehydrogenase/Electron-Transferring Flavoprotein Complex from Clostridium difficile on Butyrate Production in Escherichia coli
inferredcites →https://doi.org/10.1128/jb.00440-17openalex-snapshot
Defining Electron Bifurcation in the Electron-Transferring Flavoprotein Family
inferredcites →https://doi.org/10.1128/jb.00612-10openalex-snapshot
NADP + Reduction with Reduced Ferredoxin and NADP + Reduction with NADH Are Coupled via an Electron-Bifurcating Enzyme Complex in Clostridium kluyveri
inferredcites →https://doi.org/10.1128/jb.00678-13openalex-snapshot
NADP-Specific Electron-Bifurcating [FeFe]-Hydrogenase in a Functional Complex with Formate Dehydrogenase in Clostridium autoethanogenum Grown on CO
inferredcites →https://doi.org/10.1128/jb.01417-07openalex-snapshot
Coupled Ferredoxin and Crotonyl Coenzyme A (CoA) Reduction with NADH Catalyzed by the Butyryl-CoA Dehydrogenase/Etf Complex from Clostridium kluyveri
inferredcites →https://doi.org/10.1128/jb.01422-07openalex-snapshot
Energy Conservation via Electron-Transferring Flavoprotein in Anaerobic Bacteria
inferredcites →https://doi.org/10.1128/jb.01582-08openalex-snapshot
The Iron-Hydrogenase of Thermotoga maritima Utilizes Ferredoxin and NADH Synergistically: a New Perspective on Anaerobic Hydrogen Production
inferredcites →https://doi.org/10.1128/jb.01839-14openalex-snapshot
Evidence for a Hexaheteromeric Methylenetetrahydrofolate Reductase in Moorella thermoacetica
inferredcites →https://doi.org/10.1128/jb.02158-12openalex-snapshot
A Reversible Electron-Bifurcating Ferredoxin- and NAD-Dependent [FeFe]-Hydrogenase (HydABC) in Moorella thermoacetica
inferredcites →https://doi.org/10.1128/mbio.02285-16openalex-snapshot
A Ferredoxin- and F 420 H 2 -Dependent, Electron-Bifurcating, Heterodisulfide Reductase with Homologs in the Domains Bacteria and Archaea
inferredcites →https://doi.org/10.1146/annurev-micro-090816-093440openalex-snapshot
Electron Bifurcation: A Long-Hidden Energy-Coupling Mechanism
inferredcites →https://doi.org/10.2210/pdb6hlm/pdbopenalex-snapshot
Variant G129D of NuoEF from Aquifex aeolicus bound to NAD+
inferredcites →https://doi.org/10.3389/fmicb.2012.00137openalex-snapshot
The membrane QmoABC complex interacts directly with the dissimilatory adenosine 5′-phosphosulfate reductase in sulfate reducing bacteria
inferredcites →https://doi.org/10.3389/fmicb.2018.00401openalex-snapshot
Flavin-Based Electron Bifurcation, Ferredoxin, Flavodoxin, and Anaerobic Respiration With Protons (Ech) or NAD+ (Rnf) as Electron Acceptors: A Historical Review
inferredcites →https://doi.org/10.3389/fmicb.2018.01357openalex-snapshot
On the Natural History of Flavin-Based Electron Bifurcation
inferredcites →https://doi.org/10.3389/fmicb.2019.00373openalex-snapshot
Distribution, Evolution, Catalytic Mechanism, and Physiological Functions of the Flavin-Based Electron-Bifurcating NADH-Dependent Reduced Ferredoxin: NADP+ Oxidoreductase
inferredcites →https://doi.org/10.7717/peerj.1515openalex-snapshot
Occurrence of ferredoxin:NAD + oxidoreductase activity and its ion specificity in several Gram-positive and Gram-negative bacteria

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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To, Dated: 23-12-2023dabco-Based Ionic Liquids Catalyzed Synthesis of N,N′- Substituted-Bis-(2-Nitrophenyl Amines)
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Electron‐Bifurcating Hydrogenases
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Normal vs. Inverted Ordering of Reduction Potentials in [FeFe]‐Hydrogenases Biomimetics: Effect of the Dithiolate Bulk
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Molecular strategies for flux control in an electron bifurcation protein
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CO2 fixation in anaerobic biological treatment: amorphous carbon formation driven by electron bifurcation
inferred← citeshttps://doi.org/10.1016/j.abb.2021.108908openalex-snapshot
Current topics in flavins and flavoproteins (Proceedings of the 20th nternational symposium on flavins and flavoproteins)
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The dyad of the Y-junction- and a flavin module unites diverse redox enzymes
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Unsaturated fatty acid synthesis in bacteria: Mechanisms and regulation of canonical and remarkably noncanonical pathways
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Electron bifurcation reactions in dark fermentation: An overview for better understanding and improvement
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19F NMR probes of conformational change in a bifurcating electron transfer flavoprotein
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Energy transduction by reversible electron bifurcation
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Multielectron transfer sensitization of flavin cofactor recycling
inferred← citeshttps://doi.org/10.1016/j.jbc.2022.101733openalex-snapshot
Contrasting roles for two conserved arginines: Stabilizing flavin semiquinone or quaternary structure, in bifurcating electron transfer flavoproteins
inferred← citeshttps://doi.org/10.1016/j.jbc.2022.102598openalex-snapshot
Redox properties and PAS domain structure of the Escherichia coli energy sensor Aer indicate a multistate sensing mechanism
inferred← citeshttps://doi.org/10.1016/j.jbc.2025.108453openalex-snapshot
Flavin transferase ApbE: From discovery to applications
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2025.113051openalex-snapshot
Differential ligation alters electronic state and coupling signals of iron-sulfur clusters in flavin-based electron bifurcation
inferred← citeshttps://doi.org/10.1016/j.rser.2024.115166openalex-snapshot
Coupling electron bifurcation and interspecies electron transfer to mitigate ammonia and acids inhibition
inferred← citeshttps://doi.org/10.1021/acs.biochem.3c00473openalex-snapshot
Characterization of the Membrane-Associated Electron-Bifurcating Flavoenzyme EtfABCX from the Hyperthermophilic Bacterium Thermotoga maritima
inferred← citeshttps://doi.org/10.1021/acs.biochem.6c00512openalex-snapshot
A New Family of Electron-Bifurcating Enzymes Represented by Ferredoxin- and NAD-Dependent Glycerol-3-Phosphate Oxidoreductase
inferred← citeshttps://doi.org/10.1021/acs.jcim.2c00858openalex-snapshot
Machine Learning for Efficient Prediction of Protein Redox Potential: The Flavoproteins Case
inferred← citeshttps://doi.org/10.1021/acscatal.2c00316openalex-snapshot
How a Formate Dehydrogenase Responds to Oxygen: Unexpected O 2 Insensitivity of an Enzyme Harboring Tungstopterin, Selenocysteine, and [4Fe–4S] Clusters
inferred← citeshttps://doi.org/10.1039/d5sc02960kopenalex-snapshot
The influence of protein electrostatics on potential inversion in flavoproteins
inferred← citeshttps://doi.org/10.1073/pnas.2117882119openalex-snapshot
An uncharacteristically low-potential flavin governs the energy landscape of electron bifurcation
inferred← citeshttps://doi.org/10.1073/pnas.2318969121openalex-snapshot
Ferredoxin reduction by hydrogen with iron functions as an evolutionary precursor of flavin-based electron bifurcation
inferred← citeshttps://doi.org/10.1073/pnas.2501900122openalex-snapshot
An electron-bifurcating “plug” to a protein nanowire in tungsten-dependent aldehyde detoxification
inferred← citeshttps://doi.org/10.1080/00032719.2023.2174131openalex-snapshot
Structural Factors and Electron Transfer Mechanisms in Flavoenzymes
inferred← citeshttps://doi.org/10.1111/1462-2920.70394openalex-snapshot
Putative Mechanisms for Initial Reaction of Anaerobic Benzene Degradation Presumably Involving a Flavoprotein
inferred← citeshttps://doi.org/10.1126/sciadv.abm7546openalex-snapshot
Structure and electron transfer pathways of an electron-bifurcating NiFe-hydrogenase
inferred← citeshttps://doi.org/10.2174/0115701786359672241226141225openalex-snapshot
DABCO-Based Ionic Liquids: A Non-Conventional Catalyst for the Synthesis of N-Substituted 2-Nitrophenylamines
inferred← citeshttps://doi.org/10.32885/2220-0975-2022-4-126-144openalex-snapshot
Electron-donor and regulatory effects of superoxide anion radicals on the processes of osteogenesis and bone remodeling: literature review
inferred← citeshttps://doi.org/10.3389/fmicb.2021.703525openalex-snapshot
Energy Conservation in Fermentations of Anaerobic Bacteria
inferred← citeshttps://doi.org/10.3390/metabo12090823openalex-snapshot
Site-Differentiated Iron–Sulfur Cluster Ligation Affects Flavin-Based Electron Bifurcation Activity
inferred← citeshttps://doi.org/10.4018/978-1-6684-7198-2.ch015openalex-snapshot
Versatility and Specificity of Flavin-Based Oxidoreductases in the Electron Transfer Reactions
inferred← citeshttps://doi.org/10.7554/elife.77095openalex-snapshot
Structure-based electron-confurcation mechanism of the Ldh-EtfAB complex
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