Bases moléculaires de la catalyse rédox
Molecular bases of redox catalysis
Publications
2025
Iago A. Modenez, Anabella Ivancich, Vincent L. Pecoraro.
De Novo design of α-helical heme binding proteins capable of versatile cofactor ligation.
Methods Enzymol., 2025, 720, 115-139.
DOI: 10.1016/bs.mie.2025.07.013
HAL: hal-05236072
Chloé Truong, Nil Gaudu, Orion Farr, Adriana Clouet, Daniel Ferry, François Guyot, Georges Ona-Nguema, Christian Ruby, Wolfgang Nitschke, Olivier Grauby, Simon Duval.
Fe2+ disproportionation within iron-rich alkaline vent analogues reveals proto-bioenergetic systems.
Nat Commun, 2025, 16 (1).
DOI: 10.1038/s41467-025-65716-w
HAL: hal-05385902
Wouter Versantvoort, Rainer Hienerwadel, Christina Ferousi, Pieter van der Velden, Catherine Berthomieu, Laura van Niftrik, Frauke Baymann.
Spectroscopic insights into the mechanism of anammox hydrazine synthase.
Journal of Biological Chemistry, 2025, 301 (11), 110771 –.
DOI: 10.1016/j.jbc.2025.110771
HAL: hal-05365182
Antoine Jacob-Villedieu, Sriram Katipamula, Achille Marchand, Bertrand Reuillard, Vincent Artero, Vincent Fourmond, Bruno Faure, A. Jalila Simaan, Christophe Léger.
Substituting Cyclohexyl with Phenyl at Phosphorus Makes a NiP₂N₂ Molecular Catalyst Active for Hydrogen Evolution in Alkaline Conditions at Low Overvoltage.
J. Am. Chem. Soc., 2025.
DOI: 10.1021/jacs.5c11615
HAL: hal-05318786
Dawit T. Filmon, Jan Jaenecke, Martin Winkler, Vincent Fourmond, Christophe Léger, Nicolas Plumeré.
Turning the FeFe hydrogenase from Clostridium beijerinckii into an efficient H2 oxidation catalyst using a redox-active matrix.
Proc. Natl. Acad. Sc. USA, 2025, 122 (41), e2514698122.
DOI: 10.1073/pnas.2514698122
HAL: hal-05306583
(dataset available here)
Vincent Fourmond, Antoine Jacob-Villedieu, A. Jalila Simaan, Bruno Faure, Christophe Léger.
Unimolecular and Bimolecular Pathways in Bidirectional Redox Molecular Catalysis.
J. Am. Chem. Soc., 2025, 147 (39), 35788–35800.
DOI: 10.1021/jacs.5c12075
HAL: hal-05270450v1
Wolfgang Nitschke, Simon Duval.
Book: Metal Ions and the Route to Life.
Book: Metal Ions and the Route to Life (Ed by Wolfgang Nitschke and Simon Duval), 2025.
DOI: 10.1201/9781003459910
HAL: hal-05338523
Orion Farr, Nil Gaudu, Adriana Clouet, Michael J. Russell, Chloé Truong.
Fe-Oxyhydroxide “Fougerite/Green Rust” Minerals Transformed (or Proto-metabolized) CO2 and CH4 Prior to Life’s Emergence.
Metal Ions and the Route to Life (Ed by Wolfgang Nitschke and Simon Duval), 2025, 309 – 340.
DOI: 10.1201/9781003459910-8
HAL: hal-05338504
Ana Rita Oliveira, Guilherme Vilela-Alves, Cristiano Mota, Christophe Léger, Vincent Fourmond, Frédéric Biaso, Bruno Guigliarelli, Maria João Romão, Inês A. Cardoso Pereira.
The Role of Selenocysteine in Catalysis and Oxygen Tolerance of a W-Dependent Formate Dehydrogenase.
ACS Catal., 2025, 15 (15), 12627 – 12639.
DOI: 10.1021/acscatal.5c02382
HAL: hal-05206805v1
Umberto Contaldo, Paolo Santucci, Alexandra Vergnes, Philippe Leone, Jérôme Becam, Frédéric Biaso, Marianne Ilbert, Benjamin Ezraty, Elisabeth Lojou, Ievgen Mazurenko.
How the Larger Methionine-Rich Domain of CueO from Hafnia alvei Enhances Cuprous Oxidation.
JACS Au, 2025, 5 (4), 1833 – 1844.
DOI: 10.1021/jacsau.5c00076
HAL: hal-05030332
Miriam Malagnini, Anna Aldinio-Colbachini, Laura Opdam, Andrea di Giuliantonio, Andrea Fasano, Vincent Fourmond, Christophe Léger.
Initial quality assessment and qualitative interpretation of protein film electrochemistry catalytic data.
Bioelectrochemistry, 2025, 108967 –.
DOI: 10.1016/j.bioelechem.2025.108967
HAL: hal-04993549v1
(dataset available here)
Felix J. Elling, Fabien Pierrel, Sophie-Carole Chobert, Sophie S. Abby, Thomas W. Evans, Arthur Reveillard, Ludovic Pelosi, Juliette Schnoebelen, Jordon D. Hemingway, Ahcène Boumendjel, Kevin W. Becker, Pieter Blom, Julia Cordes, Vinitra Nathan, Frauke Baymann, Sebastian Lücker, Eva Spieck, Jared R. Leadbetter, Kai-Uwe Hinrichs, Roger E. Summons, Ann Pearson.
A novel quinone biosynthetic pathway illuminates the evolution of aerobic metabolism.
Proc. Natl. Acad. Sci. U.S.A., 2025, 122 (8).
DOI: 10.1073/pnas.2421994122
HAL: hal-04679398v2
Joel I. Badillo‐Gómez, Irene Suarez‐Antuña, Ievgen Mazurenko, Frédéric Biaso, Jacques Pécaut, Elisabeth Lojou, Pascale Delangle, Sarah Hostachy.
Biomimetic Pseudopeptides to Decipher the Interplay between Cu and Methionine‐Rich Domains in Proteins.
Chemistry A European J, 2025, e202403896.
DOI: 10.1002/chem.202403896
HAL: hal-04873808
2024
Umberto Contaldo, Dylan Savant-Aira, Alexandra Vergnes, Jérôme Becam, Frédéric Biaso, Marianne Ilbert, Laurent Aussel, Benjamin Ezraty, Elisabeth Lojou, Ievgen Mazurenko.
Methionine-rich domains emerge as facilitators of copper recruitment in detoxification systems.
Proc. Natl. Acad. Sci. U.S.A., 2024, 121 (42), e2402862121.
DOI: 10.1073/pnas.2402862121
HAL: hal-04728816
Lars J.C. Jeuken, Dennis G.H. Hetterscheid, Marc T.M. Koper, Carla Casadevall, Christophe Léger, Antoni Llobet, Ross D. Milton, Ryuhei Nakamura, Kristina Tschulik.
Toward an informative comparison of heterogeneous, synthetic, and biological electrocatalysis in energy conversion.
Chem Catalysis, 2024, 101098 –.
DOI: 10.1016/j.checat.2024.101098
HAL: hal-04691332v1
Alessia Munzone, Manon Pujol, Ashish Tamhankar, Chris Joseph, Ievgen Mazurenko, Marius Réglier, Sergio A. V. Jannuzzi, Antoine Royant, Giuseppe Sicoli, Serena DeBeer, Maylis Orio, A. Jalila Simaan, Christophe Decroos.
Integrated Experimental and Theoretical Investigation of Copper Active Site Properties of a Lytic Polysaccharide Monooxygenase from Serratia marcescens.
Inorg. Chem., 2024, 63 (24), 11063 – 11078.
DOI: 10.1021/acs.inorgchem.4c00602
HAL: hal-04595887
Andrea Fasano, Aurore Jacq-Bailly, Jeremy Wozniak, Vincent Fourmond, Christophe Léger.
Catalytic Bias and Redox-Driven Inactivation of the Group B FeFe Hydrogenase CpIII.
ACS Catal., 2024, 14 (9), 7001 – 7010.
DOI: 10.1021/acscatal.4c01352
HAL: hal-04570861v1
(dataset available here)
Andrea Fasano, Vincent Fourmond, Christophe Léger.
Outer-sphere effects on the O2 sensitivity, catalytic bias and catalytic reversibility of hydrogenases.
Chem. Sci., 2024, 15, 5418 – 5433.
DOI: 10.1039/D4SC00691G
HAL: hal-04550524v1
(dataset available here)
Andrea Fasano, Vincent Fourmond, Christophe Léger.
The difference bidirectionality makes to the kinetic modeling of molecular catalysis.
Curr. Op. Electrochem., 2024, 46, 101489.
DOI: 10.1016/j.coelec.2024.101489
HAL: hal-04550686v1
Andrea Fasano, Carole Baffert, Conrad Schumann, Gustav Berggren, James A. Birrell, Vincent Fourmond, Christophe Léger.
Kinetic Modeling of the Reversible or Irreversible Electrochemical Responses of FeFe-Hydrogenases.
J. Am. Chem. Soc., 2024, 146 (2), 1455–1466.
DOI: 10.1021/jacs.3c10693
HAL: hal-04372676v1
(dataset available here)
Ana Rita Oliveira, Cristiano Mota, Guilherme Vilela-Alves, Rita Rebelo Manuel, Neide Pedrosa, Vincent Fourmond, Kateryna Klymanska, Christophe Léger, Bruno Guigliarelli, Maria João Romão, Inês A. Cardoso Pereira.
An allosteric redox switch involved in oxygen protection in a CO2 reductase.
Nat Chem Biol, 2024, 20 (1), 111-119.
DOI: 10.1038/s41589-023-01484-2
HAL: hal-04383526
(dataset available here)
Ievgen Mazurenko, Anne de Poulpiquet, Elisabeth Lojou.
Bioélectrocatalyse impliquant des enzymes multi-cuivres.
l’Actualité Chimique, 2024, 499, 41.
(voir / see)
HAL: hal-05344574
Andrea Fasano, Vincent Fourmond, Christophe Léger.
Kinetic modeling of 2e-/1H+ and 2e-/2H+ bidirectional catalytic cycles.
Bioelectrochemistry, 2024, 108511 –.
DOI: 10.1016/j.bioelechem.2023.108511
HAL: hal-04284492
Christelle Hureau, Christophe Léger, Wadih Gattas, Isabelle Michaud-Soret, Hélène C Bertrand, Vincent Lebrun, Marine Desage-El Murr, Benoit Bertrand.
Mécanismes moléculaires autour des métaux : du vivant aux applications.
Actualité Chimique, 2024.
HAL: hal-04975335
2023
Andrea Fasano, Chloé Guendon, Aurore Jacq-Bailly, Arlette Kpebe, Jérémy Wozniak, Carole Baffert, Melisa del Barrio, Vincent Fourmond, Myriam Brugna, Christophe Léger.
A Chimeric NiFe Hydrogenase Heterodimer to Assess the Role of the Electron Transfer Chain in Tuning the Enzyme’s Catalytic Bias and Oxygen Tolerance.
J. Am. Chem. Soc., 2023, 145 (36), 20021–20030.
DOI: 10.1021/jacs.3c06895
HAL: hal-04284474
(dataset available here)
Raphaël J. Labidi, Bruno Faivre, Philippe Carpentier, Giulia Veronesi, Albert Solé-Daura, Ragnar Bjornsson, Christophe Léger, Philipp Gotico, Yun Li, Mohamed Atta, Marc Fontecave.
Light-Driven Hydrogen Evolution Reaction Catalyzed by a Molybdenum–Copper Artificial Hydrogenase.
J. Am. Chem. Soc., 2023.
DOI: 10.1021/jacs.3c01350
HAL: hal-04128647
Cheriehan Hessin, Jules Schleinitz, Nolwenn Le Breton, Sylvie Choua, Laurence Grimaud, Vincent Fourmond, Marine Desage-El Murr, Christophe Léger.
Assessing the Extent of Potential Inversion by Cyclic Voltammetry: Theory, Pitfalls, and Application to a Nickel Complex with Redox-Active Iminosemiquinone Ligands.
Inorg. Chem., 2023.
DOI: 10.1021/acs.inorgchem.2c04365
HAL: hal-04071135
Marta Meneghello, Alexandre Uzel, Marianne Broc, Rita R Manuel, Axel Magalon, Inês A. C. Pereira, Christophe Léger, Anne Walburger, Vincent Fourmond.
Electrochemical Kinetics Support a Second Coordination Sphere Mechanism in Metal‐Based Formate Dehydrogenase.
Angew Chem Int Ed, 2023.
DOI: 10.1002/anie.202212224
HAL: hal-03965660
2022
Andreas Rutz, Chandan K. Das, Andrea Fasano, Jan Jaenecke, Shanika Yadav, Ulf-Peter Apfel, Vera Engelbrecht, Vincent Fourmond, Christophe Léger, Lars V. Schäfer, Thomas Happe.
Increasing the O2 Resistance of the [FeFe]-Hydrogenase CbA5H through Enhanced Protein Flexibility.
ACS Catal., 2022, 856 – 865.
DOI: 10.1021/acscatal.2c04031
HAL: hal-03932821
Taiki Adachi, Ievgen Mazurenko, Nicolas Mano, Yuki Kitazumi, Kunishige Kataoka, Kenji Kano, Keisei Sowa, Elisabeth Lojou.
Kinetic and thermodynamic analysis of Cu2+-dependent reductive inactivation in direct electron transfer-type bioelectrocatalysis by copper efflux oxidase.
Electrochimica Acta, 2022, 429, 140987.
DOI: 10.1016/j.electacta.2022.140987
HAL: hal-03752803v1
Sven T. Stripp, Benjamin R. Duffus, Vincent Fourmond, Christophe Léger, Silke Leimkühler, Shun Hirota, Yilin Hu, Andrew Jasniewski, Hideaki Ogata, Markus W. Ribbe.
Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase.
Chem. Rev., 2022, 122 (14), 11900 – 11973.
DOI: 10.1021/acs.chemrev.1c00914
HAL: hal-03741456
Wolfgang Nitschke, Barbara Schoepp‐Cothenet, Simon Duval, Kilian Zuchan, Orion Farr, Frauke Baymann, Francesco Panico, Alessandro Minguzzi, Elbert Branscomb, Michael J. Russell.
Aqueous electrochemistry: The toolbox for life’s emergence from redox disequilibria.
Electrochemical Science Adv, 2022.
DOI: 10.1002/elsa.202100192
HAL: hal-03805068v1
2021
Christina Felbek, Federica Arrigoni, David de Sancho, Aurore Jacq-Bailly, Robert B. Best, Vincent Fourmond, Luca Bertini, Christophe Léger.
Mechanism of Hydrogen Sulfide-Dependent Inhibition of FeFe Hydrogenase.
ACS Catal., 2021, 15162 – 15176.
DOI: 10.1021/acscatal.1c04838
HAL: hal-03468382
Andrea Fasano, Henrik Land, Vincent Fourmond, Gustav Berggren, Christophe Léger.
Reversible or Irreversible Catalysis of H+/H2 Conversion by FeFe Hydrogenases.
J. Am. Chem. Soc., 2021.
DOI: 10.1021/jacs.1c09554
HAL: hal-03445761
Marta Meneghello, Christophe Léger, Vincent Fourmond.
Electrochemical studies of CO2‐reducing metalloenzymes.
Chem. Eur. J., 2021.
DOI: 10.1002/chem.202102702
HAL: hal-03358088
Matteo Sensi, Carole Baffert, Vincent Fourmond, Luca De Gioia, Luca Bertini, Christophe Léger.
Photochemistry and photoinhibition of the H-cluster of FeFe-hydrogenases.
Sustainable Energy Fuels, 2021, 5, 4248-4260.
DOI: 10.1039/D1SE00756D
HAL: hal-03358063
Vincent Fourmond, Christophe Léger.
Theoretical Understanding of the Penetration of O2 in Enzymatic Redox Polymer Films: The Case of Unidirectional Catalysis and Irreversible Inactivation in a Film of Arbitrary Thickness.
ChemElectroChem, 2021, 8 (13), 2607 – 2615.
DOI: 10.1002/celc.202100586
HAL: hal-03277147v1
Kilian Zuchan, Frauke Baymann, Carole Baffert, Myriam Brugna, Wolfgang Nitschke.
The dyad of the Y-junction- and a flavin module unites diverse redox enzymes.
Biochimica et Biophysica Acta (BBA) – Bioenergetics, 2021, 1862 (6), 148401 –.
DOI: 10.1016/j.bbabio.2021.148401
HAL: hal-03169066v1
Vincent Fourmond, Nicolas Plumeré, Christophe Léger.
Reversible catalysis.
Nat Rev Chem, 2021, 5 (5).
DOI: 10.1038/s41570-021-00268-3
HAL: hal-03215154
Steffen Hardt, Stefanie Stapf, Dawit T. Filmon, James A. Birrell, Olaf Rüdiger, Vincent Fourmond, Christophe Léger, Nicolas Plumeré.
Reversible H2 oxidation and evolution by hydrogenase embedded in a redox polymer film.
Nature Catalysis, 2021, 4, 251-258.
DOI: 10.1038/s41929-021-00586-1
HAL: hal-03215114
(dataset available here)
Marta Meneghello, Ana Rita Oliveira, Aurore Jacq-Bailly, Inês Cardoso Peirera, Christophe Léger, Vincent Fourmond.
Formate dehydrogenases reduce CO2 rather than HCO3‐: an electrochemical demonstration.
Angew. Chem. Int. Ed., 2021.
DOI: 10.1002/anie.202101167
HAL: hal-03181024
Martin Winkler, Jifu Duan, Andreas Rutz, Christina Felbek, Lisa Scholtysek, Oliver Lampret, Jan Jaenecke, Ulf-Peter Apfel, Gianfranco Gilardi, Francesca Valetti, Vincent Fourmond, Eckhard Hofmann, Christophe Léger, Thomas Happe.
A safety cap protects hydrogenase from oxygen attack.
Nat Commun, 2021, 12 (1).
DOI: 10.1038/s41467-020-20861-2
HAL: hal-03129104
Aurore Jacq-Bailly, Martino Benvenuti, Natalie Payne, Arlette Kpebe, Christina Felbek, Vincent Fourmond, Christophe Léger, Myriam Brugna, Carole Baffert.
Electrochemical Characterization of a Complex FeFe Hydrogenase, the Electron-Bifurcating Hnd From Desulfovibrio fructosovorans.
Front. Chem., 2021, 8.
DOI: 10.3389/fchem.2020.573305
HAL: hal-03103487v1
Christina Felbek, Steffen Hardt, Cecilia Papini, Debajyoti Pramanik, Vincent Artero, Marc Fontecave, Vincent Fourmond, Nicolas Plumere, Christophe Léger.
Artificial maturation of [FeFe] hydrogenase in a redox polymer film.
Chem. Commun., 2021.
DOI: 10.1039/D0CC08168J
HAL: hal-03102775v1
Romain Clément, Xie Wang, Frédéric Biaso, Marianne Ilbert, Ievgen Mazurenko, Elisabeth Lojou.
Mutations in the coordination spheres of T1 Cu affect Cu2+-activation of the laccase from Thermus thermophilus.
Biochimie, 2021, 182, 228-237.
DOI: 10.1016/j.biochi.2021.01.006
HAL: hal-03127150v1
2020
Vivek Pratap Hitaishi, Romain Clément, Ludovica Quattrocchi, Philippe Parent, David Duché, Lisa Zuily, Marianne Ilbert, Elisabeth Lojou, Ievgen Mazurenko.
Interplay between Orientation at Electrodes and Copper Activation of Thermus thermophilus Laccase for O2 Reduction.
J. Am. Chem. Soc., 2020, 142 (3), 1394 – 1405.
DOI: 10.1021/jacs.9b11147
HAL: hal-02503732v1
2019
Christina Ferousi, Simon Lindhoud, Frauke Baymann, Eric R. Hester, Joachim Reimann, Boran Kartal.
Discovery of a functional, contracted heme-binding motif within a multiheme cytochrome.
J. Biol. Chem., 2019, 261 (45), 1126 – 16965.
DOI: 10.1074/jbc.RA119.010568
HAL: hal-02369902v1
Xie Wang, Romain Clément, Magali Roger, Marielle Bauzan, Ievgen Mazurenko, Anne de Poulpiquet, Marianne Ilbert, Elisabeth Lojou.
Bacterial Respiratory Chain Diversity Reveals a Cytochrome c Oxidase Reducing O2 at Low Overpotentials.
J. Am. Chem. Soc., 2019, 141 (28), 11093 – 11102.
DOI: 10.1021/jacs.9b03268
HAL: hal-02160924v1
2018
Frauke Baymann, Barbara Schoepp-Cothenet, Simon Duval, Marianne Guiral, Myriam Brugna, Carole Baffert, Michael J. Russell, Wolfgang Nitschke.
On the Natural History of Flavin-Based Electron Bifurcation.
Front. Microbiol., 2018, 8, 357 –.
DOI: 10.3389/fmicb.2018.01357
HAL: hal-01828959v1
2016
Sebastian Veit, Kazuki Takeda, Yuichi Tsunoyama, Frauke Baymann, Reinat Nevo, Ziv Reich, Matthias Rögner, Kunio Miki, Sascha Rexroth.
Structural and functional characterisation of the cyanobacterial PetC3 Rieske protein family.
Biochimica et Biophysica Acta (BBA) – Bioenergetics, 2016, 1857 (12), 1879 – 1891.
DOI: 10.1016/j.bbabio.2016.09.007
HAL: hal-01441855v1
Wei-Chun Kao, Thomas Kleinschroth, Wolfgang Nitschke, Frauke Baymann, Yashvin Neehaul, Petra Hellwig, Sebastian Richers, Janet Vonck, Michael Bott, Carola Hunte.
The obligate respiratory supercomplex from Actinobacteria.
Biochimica et Biophysica Acta (BBA) – Bioenergetics, 2016, 1857 (10), 1705 – 1714.
DOI: 10.1016/j.bbabio.2016.07.009
HAL: hal-01415865v1
Lucie Bergdoll, Felix ten Brink, Wolfgang Nitschke, Daniel Picot, Frauke Baymann.
From low- to high-potential bioenergetic chains: Thermodynamic constraints of Q-cycle function.
Biochimica et Biophysica Acta (BBA) – Bioenergetics, 2016, 1857 (9), 1569 – 1579.
DOI: 10.1016/j.bbabio.2016.06.006
HAL: hal-01413250v1
2014
Anne-Lise Ducluzeau, Barbara Schoepp-Cothenet, Robert van Lis, Frauke Baymann, Michael J. Russell, Wolfgang Nitschke.
The evolution of respiratory O 2 /NO reductases: an out-of-the-phylogenetic-box perspective.
J. R. Soc. Interface, 2014, 265 (98), 11 535 –.
DOI: 10.1098/rsif.2014.0196
HAL: hal-01494539v1
2013
Barbara Schoepp-Cothenet, Robert van Lis, Ariane Atteia, Frauke Baymann, Line Capowiez, Anne-Lise Ducluzeau, Simon Duval, Felix ten Brink, Michael J. Russell, Wolfgang Nitschke.
On the universal core of bioenergetics.
Biochimica et Biophysica Acta (BBA) – Bioenergetics, 2013, 1827 (2), 79 – 93.
DOI: 10.1016/j.bbabio.2012.09.005
HAL: hal-01606377v1
Olga Kolaj-Robin, Mohamed R. Noor, Sarah R. O’Kane, Frauke Baymann, Tewfik Soulimane.
Atypical Features of Thermus thermophilus Succinate:Quinone Reductase.
PLoS ONE, 2013, 43 (1), 1441 –.
DOI: 10.1371/journal.pone.0053559
2011
Olga Kolaj-Robin, Sarah R. O’Kane, Wolfgang Nitschke, Christophe Léger, Frauke Baymann, Tewfik Soulimane.
Biochemical and biophysical characterization of succinate: Quinone reductase from Thermus thermophilus.
Biochimica et Biophysica Acta (BBA) – Bioenergetics, 2011, 1807 (1), 68 – 79.
DOI: 10.1016/j.bbabio.2010.10.009
HAL: hal-00999887v1
2009
B. Schoepp-Cothenet, C. Lieutaud, F. Baymann, A. Vermeglio, T. Friedrich, D. M. Kramer, W. Nitschke.
Menaquinone as pool quinone in a purple bacterium.
Proceedings of the National Academy of Sciences, 2009, 5 (3), 151 – 8554.
DOI: 10.1073/pnas.0813173106
2008
A.L. Ducluzeau, E. Chenu, L. Capowiez, F. Baymann.
The Rieske/cytochrome b complex of Heliobacteria.
Biochimica et Biophysica Acta (BBA) – Bioenergetics, 2008, 1777 (9), 1140 – 1146.
DOI: 10.1016/j.bbabio.2008.04.026
2007
Daniel Muller, Claudine Médigue, Sandrine Koechler, Valérie Barbe, Mohamed Barakat, Emmanuel Talla, Violaine Bonnefoy, Evelyne Krin, Florence Arsène-Ploetze, Christine Carapito, Michael Chandler, Benoît Cournoyer, Stéphane Cruveiller, Caroline Dossat, Sim.
A Tale of Two Oxidation States: Bacterial Colonization of Arsenic-Rich Environments.
PLoS Genet, 2007, 73 (4), 1917 –.
DOI: 10.1371/journal.pgen.0030053
HAL: hal-00340034v1
2004
F. Baymann, E. Lebrun, W. Nitschke.
Mitochondrial cytochrome c1 is a collapsed di-heme cytochrome.
Proceedings of the National Academy of Sciences, 2004, 179 (5), 1734 – 17740.
DOI: 10.1073/pnas.0407442101
2003
Michael Schütz, Barbara Schoepp-Cothenet, Elisabeth Lojou, Mireille Woodstra, Doris Lexa, Pascale Tron, Alain Dolla, Marie-Claire Durand, Karl Otto Stetter, Frauke Baymann.
The Naphthoquinol Oxidizing Cytochrome bc 1 Complex of the Hyperthermophilic Knallgasbacterium Aquifex aeolicus : Properties and Phylogenetic Relationships †.
Biochemistry, 2003, 42 (36), 10800 – 10808.
DOI: 10.1021/bi034452a
Frauke Baymann, Nicola L Barlow, Corinne Aubert, Barbara Schoepp-Cothenet, Gisele Leroy, Fraser A Armstrong.
Voltammetry of a ‘protein on a rope’.
2003, 9 (1-3), 48 – 94.
DOI: 10.1016/S0014-5793(03)00206-0
HAL: hal-03623212v1
Frauke Baymann, Evelyne Lebrun, Myriam Brugna, Barbara Schoepp–Cothenet, Marie–Thérèse Giudici–Orticoni, Wolfgang Nitschke.
The redox protein construction kit: pre-last universal common ancestor evolution of energy-conserving enzymes.
Phil. Trans. R. Soc. Lond. B, 2003, 180 (1429), 1460 – 274.
DOI: 10.1098/rstb.2002.1184
HAL: hal-00343715v1
2001
Frauke Baymann, Fabrice Rappaport, Pierre Joliot, Toivo Kallas.
Rapid Electron Transfer to Photosystem I and Unusual Spectral Features of Cytochrome c 6 in Synechococcus sp. PCC 7002 in Vivo †.
Biochemistry, 2001, 40 (35), 10570 – 10577.
DOI: 10.1021/bi010194a
Barbara Schoepp-Cothenet, Michael Schütz, Frauke Baymann, Myriam Brugna, Wolfgang Nitschke, Hannu Myllykallio, Christian Schmidt.
The membrane-extrinsic domain of cytochrome b 558/566 from the Archaeon Sulfolobus acidocaldarius performs pivoting movements with respect to the membrane surface.
2001, 16 (3), 544 – 376.
DOI: 10.1016/S0014-5793(00)02357-7
1999
Catherine de Vitry, Giovanni Finazzi, Frauke Baymann, Toivo Kallas.
Analysis of the Nucleus-Encoded and Chloroplast-Targeted Rieske Protein by Classic and Site-Directed Mutagenesis of Chlamydomonas.
Plant Cell, 1999, 11 (10), 2031 – 2044.
DOI: 10.1105/tpc.11.10.2031
F. Baymann, D. E. Robertson, P. L. Dutton, W. Mäntele.
Electrochemical and Spectroscopic Investigations of the Cytochrome bc 1 Complex from Rhodobacter capsulatus.
Biochemistry, 1999, 38 (40), 13188 – 13199.
DOI: 10.1021/bi990565b
1998
Frauke Baymann, Fabrice Rappaport.
Electrostatic Interactions at the Donor Side of the Photosynthetic Reaction Center of Rhodopseudomonas v iridis.
Biochemistry, 1998, 37 (44), 15320 – 15326.
DOI: 10.1021/bi980963z
1991
Frauke Baymann, David A. Moss, Werner Mäntele.
An electrochemical assay for the characterization of redox proteins from biological electron transfer chains.
Analytical Biochemistry, 1991, 199 (2), 269 – 274.
DOI: 10.1016/0003-2697(91)90100-8