Flavins in the electron bifurcation process.
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U. Ermler | W. Buckel | K. Kayastha | S. Vitt | Stella Vitt
[1] P. Chaiyen,et al. Rapid kinetics reveal surprising flavin chemistry in bifurcating electron transfer flavoprotein from Acidaminococcus fermentans , 2020, The Journal of biological chemistry.
[2] U. Ermler,et al. Structural and spectroscopic characterization of a HdrA‐like subunit from Hyphomicrobium denitrificans , 2020, The FEBS journal.
[3] J. W. Peters,et al. Universal free-energy landscape produces efficient and reversible electron bifurcation , 2020, Proceedings of the National Academy of Sciences.
[4] P. Chaiyen,et al. Modulations of the reduction potentials of flavin‐based electron bifurcation complexes and semiquinone stabilities are key to control directional electron flow , 2020, The FEBS journal.
[5] C. Dahl,et al. DsrL Mediates Electron Transfer between NADH and rDsrAB in Allochromatium vinosum. , 2019, Environmental microbiology.
[6] K. Murakami,et al. Structure and function of an unusual flavodoxin from the domain Archaea , 2019, Proceedings of the National Academy of Sciences.
[7] J. Ferry,et al. Life on the thermodynamic edge: Respiratory growth of an acetotrophic methanogen , 2019, Science Advances.
[8] T. Friedrich,et al. A mechanism to prevent production of reactive oxygen species by Escherichia coli respiratory complex I , 2019, Nature Communications.
[9] U. Ermler,et al. Low potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors , 2019, Nature Communications.
[10] J. W. Peters,et al. The catalytic mechanism of electron-bifurcating electron transfer flavoproteins (ETFs) involves an intermediary complex with NAD. , 2019, Journal of Biological Chemistry.
[11] Haiyan Huang,et al. Distribution, Evolution, Catalytic Mechanism, and Physiological Functions of the Flavin-Based Electron-Bifurcating NADH-Dependent Reduced Ferredoxin: NADP+ Oxidoreductase , 2019, Front. Microbiol..
[12] Volker Müller,et al. Electron Bifurcation: A Long-Hidden Energy-Coupling Mechanism. , 2018, Annual review of microbiology.
[13] Michael J. Russell,et al. On the Natural History of Flavin-Based Electron Bifurcation , 2018, Front. Microbiol..
[14] R. Thauer,et al. Flavin-Based Electron Bifurcation, Ferredoxin, Flavodoxin, and Anaerobic Respiration With Protons (Ech) or NAD+ (Rnf) as Electron Acceptors: A Historical Review , 2018, Front. Microbiol..
[15] J. W. Peters,et al. Distinct properties underlie flavin-based electron bifurcation in a novel electron transfer flavoprotein FixAB from Rhodopseudomonas palustris , 2018, The Journal of Biological Chemistry.
[16] U. Ermler,et al. Molecular basis of the flavin‐based electron‐bifurcating caffeyl‐CoA reductase reaction , 2018, FEBS letters.
[17] R. Rachel,et al. One-megadalton metalloenzyme complex in Geobacter metallireducens involved in benzene ring reduction beyond the biological redox window , 2018, Proceedings of the National Academy of Sciences.
[18] M. Fraaije,et al. Same Substrate, Many Reactions: Oxygen Activation in Flavoenzymes. , 2018, Chemical reviews.
[19] U. Ermler,et al. The semiquinone swing in the bifurcating electron transferring flavoprotein/butyryl-CoA dehydrogenase complex from Clostridium difficile , 2017, Nature Communications.
[20] Peng Zhang,et al. Electron Bifurcation: Thermodynamics and Kinetics of Two-Electron Brokering in Biological Redox Chemistry. , 2017, Accounts of chemical research.
[21] S. Shima,et al. Methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction , 2017, Science.
[22] J. W. Peters,et al. Defining Electron Bifurcation in the Electron-Transferring Flavoprotein Family , 2017, Journal of bacteriology.
[23] J. W. Peters,et al. The Electron Bifurcating FixABCX Protein Complex from Azotobacter vinelandii: Generation of Low-Potential Reducing Equivalents for Nitrogenase Catalysis. , 2017, Biochemistry.
[24] J. W. Peters,et al. Two functionally distinct NADP+-dependent ferredoxin oxidoreductases maintain the primary redox balance of Pyrococcus furiosus , 2017, The Journal of Biological Chemistry.
[25] P. King,et al. Equilibrium and ultrafast kinetic studies manipulating electron transfer: A short-lived flavin semiquinone is not sufficient for electron bifurcation , 2017, The Journal of Biological Chemistry.
[26] J. W. Peters,et al. Mechanistic insights into energy conservation by flavin-based electron bifurcation. , 2017, Nature chemical biology.
[27] W. Martin,et al. Energy in Ancient Metabolism , 2017, Cell.
[28] J. Ferry,et al. A Ferredoxin- and F420H2-Dependent, Electron-Bifurcating, Heterodisulfide Reductase with Homologs in the Domains Bacteria and Archaea , 2017, mBio.
[29] N. Scrutton,et al. Sweating the assets of flavin cofactors: new insight of chemical versatility from knowledge of structure and mechanism. , 2016, Current opinion in structural biology.
[30] S. Shima,et al. The methanogenic CO2 reducing-and-fixing enzyme is bifunctional and contains 46 [4Fe-4S] clusters , 2016, Science.
[31] S. de Vries,et al. The multitude of iron-sulfur clusters in respiratory complex I. , 2016, Biochimica et biophysica acta.
[32] A. Seubert,et al. Reduction of Flavodoxin by Electron Bifurcation and Sodium Ion-dependent Reoxidation by NAD+ Catalyzed by Ferredoxin-NAD+ Reductase (Rnf)* , 2016, The Journal of Biological Chemistry.
[33] M. Malamy,et al. Occurrence of ferredoxin:NAD+ oxidoreductase activity and its ion specificity in several Gram-positive and Gram-negative bacteria , 2016, PeerJ.
[34] W. Buckel,et al. Reduction of ferredoxin or oxygen by flavin‐based electron bifurcation in Megasphaera elsdenii , 2015, The FEBS Journal.
[35] R. Thauer,et al. Insights into Flavin-based Electron Bifurcation via the NADH-dependent Reduced Ferredoxin:NADP Oxidoreductase Structure* , 2015, The Journal of Biological Chemistry.
[36] J. Wall,et al. The FlxABCD-HdrABC proteins correspond to a novel NADH dehydrogenase/heterodisulfide reductase widespread in anaerobic bacteria and involved in ethanol metabolism in Desulfovibrio vulgaris Hildenborough. , 2015, Environmental microbiology.
[37] V. Müller,et al. A novel mode of lactate metabolism in strictly anaerobic bacteria. , 2015, Environmental microbiology.
[38] R. Thauer,et al. Evidence for a Hexaheteromeric Methylenetetrahydrofolate Reductase in Moorella thermoacetica , 2014, Journal of bacteriology.
[39] U. Ermler,et al. Studies on the Mechanism of Electron Bifurcation Catalyzed by Electron Transferring Flavoprotein (Etf) and Butyryl-CoA Dehydrogenase (Bcd) of Acidaminococcus fermentans* , 2013, The Journal of Biological Chemistry.
[40] Klaus Schulten,et al. The mechanism of ubihydroquinone oxidation at the Qo-site of the cytochrome bc1 complex. , 2013, Biochimica et biophysica acta.
[41] R. Thauer,et al. NADP-Specific Electron-Bifurcating [FeFe]-Hydrogenase in a Functional Complex with Formate Dehydrogenase in Clostridium autoethanogenum Grown on CO , 2013, Journal of bacteriology.
[42] W. Buckel,et al. Effect of an Oxygen-Tolerant Bifurcating Butyryl Coenzyme A Dehydrogenase/Electron-Transferring Flavoprotein Complex from Clostridium difficile on Butyrate Production in Escherichia coli , 2013, Journal of bacteriology.
[43] C. Eberlein,et al. Identification and characterization of 2‐naphthoyl‐coenzyme A reductase, the prototype of a novel class of dearomatizing reductases , 2013, Molecular microbiology.
[44] Kyosuke Sato,et al. Interaction between NADH and electron-transferring flavoprotein from Megasphaera elsdenii. , 2013, Journal of biochemistry.
[45] V. Müller,et al. An Electron-bifurcating Caffeyl-CoA Reductase* , 2013, The Journal of Biological Chemistry.
[46] R. Thauer,et al. Energy conservation via electron bifurcating ferredoxin reduction and proton/Na(+) translocating ferredoxin oxidation. , 2013, Biochimica et biophysica acta.
[47] R. Thauer,et al. A Reversible Electron-Bifurcating Ferredoxin- and NAD-Dependent [FeFe]-Hydrogenase (HydABC) in Moorella thermoacetica , 2013, Journal of bacteriology.
[48] V. Müller,et al. A Bacterial Electron-bifurcating Hydrogenase* , 2012, The Journal of Biological Chemistry.
[49] W. Martin. Hydrogen, metals, bifurcating electrons, and proton gradients: The early evolution of biological energy conservation , 2012, FEBS letters.
[50] J. Wall,et al. The Membrane QmoABC Complex Interacts Directly with the Dissimilatory Adenosine 5′-Phosphosulfate Reductase in Sulfate Reducing Bacteria , 2012, Front. Microbio..
[51] M. Russell,et al. Redox bifurcations: Mechanisms and importance to life now, and at its origin , 2012, BioEssays : news and reviews in molecular, cellular and developmental biology.
[52] Anne-Kristin Kaster,et al. Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in hydrogenotrophic methanogenic archaea , 2011, Proceedings of the National Academy of Sciences.
[53] R. Thauer,et al. NADP+ Reduction with Reduced Ferredoxin and NADP+ Reduction with NADH Are Coupled via an Electron-Bifurcating Enzyme Complex in Clostridium kluyveri , 2010, Journal of bacteriology.
[54] J. Leigh,et al. Protein complexing in a methanogen suggests electron bifurcation and electron delivery from formate to heterodisulfide reductase , 2010, Proceedings of the National Academy of Sciences.
[55] M. Adams,et al. The Iron-Hydrogenase of Thermotoga maritima Utilizes Ferredoxin and NADH Synergistically: a New Perspective on Anaerobic Hydrogen Production , 2009, Journal of bacteriology.
[56] M. Byrdin,et al. What makes the difference between a cryptochrome and DNA photolyase? A spectroelectrochemical comparison of the flavin redox transitions. , 2009, Journal of the American Chemical Society.
[57] Anne-Kristin Kaster,et al. Methanogenic archaea: ecologically relevant differences in energy conservation , 2008, Nature Reviews Microbiology.
[58] E. Jayamani,et al. Energy Conservation via Electron-Transferring Flavoprotein in Anaerobic Bacteria , 2007, Journal of bacteriology.
[59] Fuli Li,et al. Coupled Ferredoxin and Crotonyl Coenzyme A (CoA) Reduction with NADH Catalyzed by the Butyryl-CoA Dehydrogenase/Etf Complex from Clostridium kluyveri , 2007, Journal of bacteriology.
[60] N. Scrutton,et al. Dynamics driving function − new insights from electron transferring flavoproteins and partner complexes , 2007, The FEBS journal.
[61] R. Swenson,et al. Modulation of the redox properties of the flavin cofactor through hydrogen-bonding interactions with the N(5) atom: role of alphaSer254 in the electron-transfer flavoprotein from the methylotrophic bacterium W3A1. , 2007, Biochemistry.
[62] K. Jensen,et al. Thermodynamic basis of electron transfer in dihydroorotate dehydrogenase B from Lactococcus lactis: analysis by potentiometry, EPR spectroscopy, and ENDOR spectroscopy. , 2004, Biochemistry.
[63] R. Hedderich. Energy-Converting [NiFe] Hydrogenases from Archaea and Extremophiles: Ancestors of Complex I , 2004, Journal of bioenergetics and biomembranes.
[64] B. Golding,et al. Acryloyl-CoA reductase from Clostridium propionicum. An enzyme complex of propionyl-CoA dehydrogenase and electron-transferring flavoprotein. , 2003, European journal of biochemistry.
[65] D. Linder,et al. A two [4Fe-4S]-cluster-containing ferredoxin as an alternative electron donor for 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans , 2003, Archives of Microbiology.
[66] M. Sutcliffe,et al. 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* , 2001, The Journal of Biological Chemistry.
[67] G. Schneider,et al. Crystal structure of dihydropyrimidine dehydrogenase, a major determinant of the pharmacokinetics of the anti‐cancer drug 5‐fluorouracil , 2001, The EMBO journal.
[68] S. Mayhew. The effects of pH and semiquinone formation on the oxidation-reduction potentials of flavin mononucleotide. A reappraisal. , 1999, European journal of biochemistry.
[69] Lening Zhang,et al. The functions of the flavin contact residues, αArg249 and βTyr16, in human electron transfer flavoprotein , 1999 .
[70] A. Honegger,et al. Regulation of the flavin redox potential by flavin-binding antibodies. , 1997, European journal of biochemistry.
[71] M. Eren,et al. Control of oxidation-reduction potentials in flavodoxin from Clostridium beijerinckii: the role of conformation changes. , 1997, Biochemistry.
[72] Z. Zhou,et al. 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]. , 1996, Biochemistry.
[73] F. Frerman,et al. Three-dimensional structure of human electron transfer flavoprotein to 2.1-A resolution. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[74] G. Zanetti,et al. Analysis of the oxidation-reduction potentials of recombinant ferredoxin-NADP+ reductase from spinach chloroplasts. , 1996, European journal of biochemistry.
[75] C. Thorpe,et al. Structure and mechanism of action of the Acyl‐CoA dehydrogenases 1 , 1995, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[76] S. Djordjević,et al. Three-dimensional structure of butyryl-CoA dehydrogenase from Megasphaera elsdenii. , 1995, Biochemistry.
[77] Y. Hatefi,et al. Thermodynamic analysis of flavin in mitochondrial NADH:ubiquinone oxidoreductase (complex I). , 1994, Biochemistry.
[78] R. Thauer,et al. H2: heterodisulfide oxidoreductase complex from Methanobacterium thermoautotrophicum. Composition and properties. , 1994, European journal of biochemistry.
[79] Kurt Warncke,et al. Nature of biological electron transfer , 1992, Nature.
[80] J. Kuriyan,et al. Convergent evolution of similar function in two structurally divergent enzymes , 1991, Nature.
[81] P. Karplus,et al. Atomic structure of ferredoxin-NADP+ reductase: prototype for a structurally novel flavoenzyme family. , 1991, Science.
[82] R. Thauer,et al. Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum (strain Marburg). , 1990, European journal of biochemistry.
[83] R. Anderson,et al. Energetics of the one-electron reduction steps of riboflavin, FMN and FAD to their fully reduced forms. , 1983, Biochimica et biophysica acta.
[84] P. Mitchell,et al. The protonmotive Q cycle: A general formulation , 1975, FEBS letters.
[85] L. Sieker,et al. Structure of the oxidized form of a flavodoxin at 2.5-Angstrom resolution: resolution of the phase ambiguity by anomalous scattering. , 1972, Proceedings of the National Academy of Sciences of the United States of America.
[86] V. Massey,et al. Oxidation-reduction properties of flavodoxin from Peptostreptococcus elsdenii. , 1969, The Journal of biological chemistry.
[87] J. W. Peters,et al. Electron bifurcation. , 2016, Current opinion in chemical biology.
[88] Christopher T Walsh,et al. Flavoenzymes: versatile catalysts in biosynthetic pathways. , 2013, Natural product reports.
[89] P. Karplus,et al. Structural Aspects of Plant Ferredoxin : NADP+ Oxidoreductases , 2004, Photosynthesis Research.