Christophe Léger

Christophe Léger
Directeur de Recherche.
Laboratoire de Bioénergétique et Ingénierie des Protéines.
CNRS, 31, Chemin Joseph Aiguier, CS 70071, 13402 Marseille cedex 09

office: +33(0) 4 91 16 45 29; fax: 4 91 16 46 89 .



  • « Habilitation à diriger des recherches’’, University Aix-Marseille I, France (2007). [pdf]
  • Ph. D. Thesis of physical chemistry advised by F. Argoul at the Centre de Recherche Paul Pascal, University of Bordeaux, France, (1999). [pdf]
  • D.E.A. of physical chemistry with distinction. University of Bordeaux (1995).
  • “Agrégation” of chemistry (advanced teaching diploma). This is a national competitive exam to be a teacher. Rank : 59th among 1000 candidates (1994).

Research experiences

  • Director of Research (DR1 CNRS 16th section, chemical biology).
  • 2002- “Chargé de recherches” (researcher) at the lab of Bioenergetics and engineering of proteins, CNRS Marseille. [Lab pages]
  • Post doctoral research on bioelectrochemistry in the group of Fraser Armstrong, Inorganic Chemistry Laboratory, Oxford, UK (1999-2002).
  • Ph. D. at the Centre de Recherche Paul Pascal : Experimental and theoretical study of morphological instabilities in electrochemical systems.


  • President (2014-2022), then vice-president (2022-2024) of the French CNRS Research Network on Bioinorganic Chemistry (GIS FrenchBIC)
  • Board member of the Solar Fuels French network (GDR Solar fuels) (2015-)
  • President of the Bioinorganic Chemistry group of the French Chemical Society (Groupe Francais de chimie bioinorganique) (2019-)
  • Full member of the Physical-chemistry group of the “Comité National des Universités” (membre nommé titulaire en Section 31) (2019-2023).




121. A Fasano, A Bailly, J Wozniak, V Fourmond, C Léger « Catalytic bias and redox-driven inactivation of the group B FeFe hydrogenase CpIII » ACS Catalysis, (2024) in press. doi: 10.1021/acscatal.4c01352 [Dataset doi: 10.5281/zenodo.10948191] Formerly « Catalytic bias and redox-driven inactivation of ancestral FeFe hydrogenases from group B2 ». bioRxiv, (2023). doi: 10.1101/2023.06.23.541094. [Author version on HAL

120. A. Fasano, V. Fourmond and C. Léger, « The difference bidirectionality makes to the kinetic modeling of molecular catalysis ». Curr Op. Electrochem. 46, 101489 (2024). doi: 10.1016/j.coelec.2024.101489  (open access) [HAL]

119. A. Fasano, V. Fourmond and C. Léger, « Outer-sphere effects on the O2 sensitivity, catalytic bias and catalytic reversibility of hydrogenases », Chem. Sc. 15, 5418-5433 (2024). doi: 10.1039/D4SC00691G (open access). [Dataset doi: 10.5281/zenodo.10849830]. Cover by Laurent Eisler. [HAL]

118. 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. 20 (1), 111-119 (2024). doi: 10.1038/s41589-023-01484-2 [Author version on HAL]

117. A. Fasano, C. Baffert, C. Schumann, G Berggren, J. Birrell, V. Fourmond, C. Léger, « Kinetic modeling of the reversible or irreversible electrochemical responses of FeFe-hydrogenases », J. Am. Chem. Soc 146, 2, 1455–1466 (2024) doi: 10.1021/jacs.3c10693. [Author version on HAL]

116. A. Fasano, V. Fourmond and C. Léger, « Kinetic modeling of 2e-/1H+ and 2e-/2H+ bidirectional catalytic cycles », Bioelectrochemistry 155, 108511 (2024). doi: 10.1016/j.bioelechem.2023.108511 (open access) [HAL]


115. A. Fasano, C. Guendon, A. Jacq-Bailly, A. Kpebe, J. Wozniak, C. Baffert, M. del Barrio, V. Fourmond, M. Brugna*, C. 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. 145, 36, 20021–20030 (2023). doi: 10.1021/jacs.3c06895  (CNRS: en direct des labos) (Infuse AMU) [Author version on HAL]

114. R. Labidi, B. Faivre, Ph. Carpentier, G. Veronesi, R. Bjornsson, C. Leger, Ph. Gotico, Y. Li, M. Atta, M. Fontecave. « Light-Driven Hydrogen Evolution Reaction Catalyzed by a Molybdenum-Copper Artificial Hydrogenase », J. Am. Chem. Soc. 145, 25, 13640–13649 (2023). doi: 10.1021/jacs.3c01350 [Author version on HAL]

113.  A. Aldinio-Colbachini, A. Fasano, C. Guendon, A. Bailly, J. Wozniak, C. Baffert, A. Kpebe, C. Léger; M. Brugna; V. Fourmond, « Transport limited adsorption experiments give a new lower estimate of the turnover frequency of Escherichia coli hydrogenase », BBA Advances 3, 100090 (2023). doi: 10.1016/j.bbadva.2023.100090 (open access) [HAL]

112. C. Hessin, J. Schleinitz, N. Le Breton, S. Choua, L. Grimaud, V. Fourmond, M.  Desage-El Murr, C. 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. (featured article) 62, 8, 3321–3332 (2023). doi: 10.1021/acs.inorgchem.2c04365. [Author version on HAL]

111. A. Rutz, C. Das, A. Fasano, J. Jaenecke, S. Yadav, U.P. Apfel, V. Engelbrecht, V. Fourmond, C. Léger, L. Schäfer, T. Happe « Increasing the O2 resistance of the [FeFe]-hydrogenase CbA5H through enhanced protein flexibility », ACS Catalysis 13, 2, 856–865 (2023) doi: 10.1021/acscatal.2c04031 [Author version on HAL]


110. Marta Meneghello, Alexandre Uzel, Marianne Broc, Rita R. Manuel, Axel Magalon, Christophe Léger, Inês A. C.Pereira, Anne Walburger, Vincent Fourmond, « Electrochemical Kinetics Support a Second Coordination Sphere Mechanism in Metal-Based Formate Dehydrogenase » Angewandte Chemie Int. Ed. (2022) e202212224 doi: 10.1002/anie.202212224 [free]

109. S. Stripp*, B. Duffus, V. Fourmond, C. Léger, S. Leimkühler, S.  Hirota, Y. Hu, A. Jasniewski, H. Ogata, M. Ribbe, « Second and Outer Coordination Sphere Effects in Low Valent Metalloenzymes », Chemical Reviews 122, 14, 11900–11973 (2022). doi: 10.1021/acs.chemrev.1c00914 [author version on HAL]


108. C. Felbek, F. Arrigoni, D. De Sancho, A. Bailly, R. Best, V.  Fourmond, L. Bertini, C. Léger*, « Mechanism of  hydrogen sulfide dependent inhibition of FeFe hydrogenase », ACS Catalysis 11, 24, 15162-15176 (2021) doi: 10.1021/acscatal.1c04838 [Author version on HAL]

107. Andrea Fasano, Henrik Land, Vincent Fourmond, Gustav Berggren, and Christophe Léger*, « Reversible or irreversible catalysis of H+/H2 conversion by FeFe hydrogenases », J. Am. Chem. Soc. 143, 48, 20320-20325 (2021) doi: 10.1021/jacs.1c09554 [Author version on HAL]

106. Marta Meneghello, Christophe Léger, Vincent Fourmond*, « Electrochemical studies of CO2-reducing metalloenzymes », Chem. Eur. J. 27, 70, 17542-17553 (2021) doi: 10.1002/chem.202102702 [Author version on HAL]

105. 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, 5, 4248-4260 (2021) doi: 10.1039/D1SE00756D [Author version on HAL]

104. Christophe Léger & Vincent Fourmond*. « Theoretical understanding of the penetration of O2 in enzymatic redox polymer films: case of unidirectional catalysis and irreversible inactivation in a film of arbitrary thickness » ChemElectroChem 8, 2607-2615 (2021) doi: 10.1002/celc.202100586 In Memoriam: Prof. Jean-Michel Savéant [Author version on HAL]

103. Vincent Fourmond, Nicolas Plumeré, Christophe Léger*, « Reversible catalysis », Nature Reviews Chemistry, 5, 348-360 (2021) doi: 10.1038/s41570-021-00268-3 [view-only published version] [author version on HAL] [ask us for the pdf of the published version]. The journal cover was designed by Laurent Eisler.

102. 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 4, 251–258 (2021)  doi: 10.1038/s41929-021-00586-1 [view-only published version] [full text on PMC after Sep. 28th 2021] [author version on HAL after Sep. 18th 2021] [ask us for the pdf of the published version]

Christophe Léger. Revised version of the article on enzyme kinetics in the French Encyclopédie Universalis (2021)

101. Marta Meneghello, Ana Rita Oliveira, Aurore Jacq-Bailly, Inês A. C. Pereira, Christophe Léger, Vincent Fourmond*, « Formate dehydrogenases reduce CO2 rather than HCO3-: an electrochemical demonstration », Angewandte Chemie Int. Ed., 60(18), 9964-9967 (2021) doi: 10.1002/anie.202101167 [Author version on HAL]

100. 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 » Nature Communications 12, 756 (2021) (open access) doi: 10.1038/s41467-020-20861-2

99. Christina Felbek, Steffen Hardt, Cecilia Papini, Debajyoti Pramanik, Vincent Artero, Marc Fontecave, Vincent Fourmond, Nicolas Plumeré, Christophe Léger* « Artificial maturation of [FeFe] hydrogenase in a redox polymer film »  Chem Comm, 57, 1750-1753 (2021) (open access) doi:10.1039/D0CC08168J

98. Aurore Jacq-Bailly, Martino Benvenuti, Natalie Rae Payne, Arlette Kpebe, Christina Felbek, Vincent Fourmond, Christophe Léger, Myriam Brugna, Carole Baffert*, Frontiers in Chemistry, vol 8, article 573305 (2020) (open access) doi:10.3389/fchem.2020.573305


97. C. Léger & V. Fourmond*, « Numerical computations of Marcus–hush–Chidsey electron transfer rate constants » J. Electroanal. Chem., 879, 114762 (2020). doi:10.1016/j.jelechem.2020.114762 [Author version on HAL]

96. E. Wittenborn, C. Guendon, M. Merrouch, M. Benvenuti, V. Fourmond, C. Léger, C. Drennan*, S. Dementin*, « The solvent-exposed Fe-S D-cluster contributes to oxygen-resistance in D. vulgaris Ni-Fe carbon monoxide dehydrogenase » ACS Catalysis, 10, 7328–7335 (2020)  doi:10.1021/acscatal.0c00934 [Free full text available on PMC after 04 Jun 2021] [HAL]

95. M Benvenuti, M Meneghello, C Guendon, A Jacq-Bailly, JH Jeoung, H Dobbek, C Léger, V Fourmond, S Dementin “The two CO-dehydrogenases of Thermococcus sp. AM4”  Biochim Biophys Acta Bioenerg. 1861, 148188 (2020). doi: 10.1016/j.bbabio.2020.148188 [Author version on HAL]


94. Huaiguang Li, Darren Buesen, Sebastien Dementin, Christophe Leger*, Vincent Fourmond*, Nicolas Plumere*, Complete Protection of O2-Sensitive Catalysts in Thin Films J. Am. Chem. Soc., 141 16734 (2019) doi:10.1021/jacs.9b06790 (open access) Highlight by David Schilter in Nat. Rev. Chem. doi:10.1038/s41570-019-0141-z 

93. Sonia Zacarias, Adriana Temporao, Melisa del Barrio, Vincent Fourmond, Christophe Léger, Pedro M. Matias, Ines A. C. Pereira*, ‘’A Hydrophilic Channel Is Involved in Oxidative Inactivation of a [NiFeSe] Hydrogenase’’, ACS Cat. 9 8509-8519 (2019) doi:10.1021/acscatal.9b02347 [HAL]

92. E. C. Wittenborn, S. E. Cohen, M. Merrouch, C. Léger, V. Fourmond, S. Dementin, C. L. Drennan* « Structural insight into metallocofactor maturation in carbon monoxide dehydrogenase », J. Biol. Chem. 294 13017 (2019) doi:10.1074/jbc.RA119.009610

91. V. Fourmond*, E. Wiedner, W. Shaw, C. Léger* “On the understanding and design of bidirectional and reversible catalysts of multielectron, multistep reactions” J. Am. Chem. Soc. 141 11269 (2019) doi:10.1021/jacs.9b04854 [Author version on HAL]

90. Melisa del Barrio, Chloe Guendon, Arlette Kpebe, Carole Baffert, Vincent Fourmond, Myriam Brugna, and Christophe Léger*, “A valine-to-cysteine mutation further increases the oxygen tolerance of Escherichia coli NiFe hydrogenase Hyd-1” ACS Catalysis 9 4084 (2019) doi:10.1021/acscatal.9b00543


89. E C Wittenborn, M Merrouch, C Ueda, L Fradale, C Léger, V Fourmond, M-E Pandelia, S Dementin, C L Drennan, “Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase”, eLife (2018) doi: 10.7554/eLife.39451

88. G Caserta, C Papini, A Adamska-Venkatesh, L Pecqueur, C Sommer, E Reijerse, W Lubitz, C Gauquelin, I Meynial-Salles, D Pramanik, V Artero, M Atta, M del Barrio, B Faivre, V Fourmond, C Léger and M Fontecave, “Engineering an [FeFe]-hydrogenase: do accessory clusters influence O2resistance and catalytic bias?”, J. Am. Chem. Soc. 140, 16, 5516–5526 (2018) doi: 10.1021/jacs.8b01689

87. M del Barrio, M Sensi, L Fradale, M Bruschi, C Greco, L de Gioia, L Bertini, V Fourmond, and C Léger, “Interaction of the H-cluster of FeFe hydrogenase with halides”, J. Am. Chem. Soc.  140, 16, 5485–5492 (2018) doi:10.1021/jacs.8b01414

86. M. Del Barrio, Melisa and M. Sensi and C. Orain and C. Baffert and S. Dementin and V. Fourmond and C. Léger, “Electrochemical investigations of hydrogenases and other enzymes that produce and use solar fuels” Acc. Chem. Res. 51 569 (2018). doi:10.1021/acs.accounts.7b00622

85. M Merrouch, M Benvenuti, M Lorenzi, C Léger, V Fourmond, S Dementin, “Maturation of the [NiFe4S4] active site of carbon monoxide dehydrogenases” J. Biol. Inorg. Chem. 23, 613–620 (2018) doi:10.1007/s00775-018-1541-0 (open access)

84. C Gauquelin, C Baffert; P Richaud, E Kamionka; E Etienne, D Guieysse, L Girbal, V Fourmond, I Andre, B Guigliarelli, C Léger, P Soucaille, I Meynial-salles. “Roles of the F-domain in [FeFe] hydrogenase”, BBA Bioenergetics 1859 69-77 (2018) doi: 10.1016/j.bbabio.2017.08.010


83. Lilith Domnik, Meriem Merrouch, Sebastian Goetzl, Jae-Hun Jeoung, Christophe Léger, Sebastien Dementin, Vincent Fourmond, Holger Dobbek, “CODH-IV: A novel high efficiency CO-scavenging CO dehydrogenase with increased resistance to O2” Angewandte Chemie Int. Ed. 56 15466-15469 (2017) doi:10.1002/anie.201709261

82. M Sensi, C Baffert, L Fradale, C Gauquelin, P Soucaille, I Meynial-Salles, H Bottin, L de Gioia, M Bruschi, V Fourmond, C Léger, L Bertini. “Photoinhibition of FeFe hydrogenase,” ACS Catalysis 7 7378-7387 (2017). doi: 10.1021/acscatal.7b02252

81. M Sensi, M del Barrio, C Baffert, V Fourmond, C Léger “New perspectives in hydrogenase direct electrochemistry”, Current Opinion in Electrochemistry, 5, 135-145 (2017) doi:10.1016/j.coelec.2017.08.005

C. Léger, contribution aux actes du Colloque “Biomimétisme et chimie durable”, 10 novembre 2015, Quelles voies de recherches pour la catalyse de l’hydrogène et la valorisation du dioxyde de carbone ? » [pdf]

80. V. Fourmond and C. Léger “N2 reduction: interfacing the enzyme nitrogenase with electrodes” Angewandte Chemie Int. Ed. 56, 4388-4390 (2017) doi:10.1002/anie.201701179

79. M. Merrouch et al, “Reliable estimation of the kinetic parameters of redox enzymes by taking into account mass transport towards rotating electrodes in protein film voltammetry experiments” Electrochimica Acta, 245, 1059-1064 (2017) 10.1016/j.electacta.2017.03.114

78. V Fourmond and C. Léger, “Modelling the voltammetry of adsorbed enzymes and molecular catalysts”, Curr. Op. Electrochem, 1:1, 110-120 (2017) doi:10.1016/j.coelec.2016.11.002

77. Adam Kubas, Christophe Orain, David De Sancho, Laure Saujet, Matteo Sensi, Mr. Charles Gauquelin, Isabelle Meynial-Salles, Philippe Soucaille, Herve Bottin, Carole Baffert, Vincent Fourmond, Robert Best, Jochen Blumberger, Christophe Léger, “Mechanism of O2 diffusion and reduction in FeFe hydrogenase”, Nature Chemistry 9, 88-95 (2017) doi: 10.1038/nchem.2592 [free to read on PMC]


76. V. Fourmond and C. Léger “Protein Electrochemistry: Questions and Answers” Adv Biochem Eng Biotechnol. (2016) DOI:10.1007/10_2015_5016

75. M Sensi, C Baffert, C Greco, G Caserta, C Gauquelin, L Saujet, M Fontecave, S Roy, V Artero, P Soucaille, I Meynial-Salles, H Bottin, L de Gioia, V Fourmond, Christophe Léger and L Bertini, “Reactivity of the excited states of the H-cluster of FeFe hydrogenases,” J. Am. Chem. Soc. 138 13612-13618 (2016) doi:10.1021/jacs.6b06603

74. Pierre Ceccaldi, Emilien Etienne, Sebastien Dementin, Bruno Guigliarelli, Christophe Léger, Benedicte Burlat, “Mechanism of inhibition of NiFe hydrogenase by nitric oxide”, BBA – Bioenergetics, 1857, 454-461( 2016).


73. M. Merrouch, J Hadj-Said, L Domnik, H. Dobbek, C. Léger, S. Dementin, V. Fourmond “Inhibition of Ni-containing CO dehydrogenase by O2 is partly reversible” Chem. Eur. J., 21, 18934-18938 (2015) doi: 10.1002/chem.201502835

72. C Orain, L Saujet, C Gauquelin, P Soucaille, I Meynial-Salles, C Baffert, V Fourmond, H Bottin, and C Léger “Electrochemical measurements of the kinetics of inhibition of two FeFe hydrogenases by O2 demonstrate that the reaction is partly reversible” J. Am. Chem. Soc. 137, 12580-12587 (2015) DOI: 10.1021/jacs.5b06934

71. J Hadj-Said, ME Pandelia, C Léger, V Fourmond, S Dementin, “The Carbon Monoxide Dehydrogenase from Desulfovibrio vulgaris” BBA – Bioenergetics 1847, 1574-1583 (2015) doi:10.1016/j.bbabio.2015.08.002

70. P Ceccaldi, M Marques, V Fourmond, I C Pereira, C Léger “Oxidative inactivation of NiFeSe hydrogenase” Chem. Commun. 51, 14223-14226 (2015) doi:10.1039/C5CC05930E

69. P Ceccaldi, J Rendon, Ch Léger, R Toci, B Guigliarelli, A Magalon, S Grimaldi, V Fourmond, “Reductive Activation of E. coli Respiratory Nitrate Reductase” BBA – Bioenergetics 1847 1055-1063 (2015) doi:10.1016/j.bbabio.2015.06.007

68. V Fourmond, S Stapf, H Li, D Buesen, J Birrell, O Rudiger, W Lubitz, W Schuhmann, N Plumere, C Léger, “The mechanism of protection of catalysts supported in redox hydrogel films” J. Am. Chem. Soc. 137 5494-5505 (2015) doi:10.1021/jacs.5b01194

67. A Abou-Hamdan, P Ceccaldi, H Lebrette, O Gutierrez-Sanz, P Richaud, L Cournac, B Guigliarelli, A L. de Lacey, C Leger, A Volbeda, B Burlat and S Dementin “A Threonine Stabilizes the NiC and NiR Catalytic Intermediates of [NiFe]-hydrogenase” J. Biol. Chem. 290 8550-8558 (2015) doi:10.1074/jbc.M114.630491

66. Carole Baffert , Sebastien Dementin , Vincent Fourmond , Christophe Léger, “L’electrochimie, un outil pour etudier les mecanismes enzymatiques”, L’actualite chimique, 392, 9-15, janvier (2015), [pdf]


65. C Greco, V Fourmond, C Baffert, P-H Wang, S Dementin, P Bertrand, M Bruschi, J Blumberger, L de Gioia, C Leger, Combining experimental and theoretical methods to learn about the reactivity of gas-processing metalloenzymes, Energy Environ. Sci., 7, 3543-3573 (2014). doi:10.1039/C4EE01848F (open access)

64. J Jacques, B Burlat, P Arnoux, M Sabaty, B Guigliarelli, C Léger, D Pignol, V Fourmond, “Kinetics of substrate inhibition of periplasmic nitrate reductase” BBA Bionergetics, 1837, 1801-1809 (2014) doi:10.1016/j.bbabio.2014.05.357

63. Vincent Fourmond, Claudio Greco, Kateryna Sybirna, Carole Baffert, Po-Hung Wang, Pierre Ezanno, Marco Montefiori, Maurizio Bruschi, Isabelle Meynial-Salles, Philippe Soucaille, Jochen Blumberger, Herve Bottin, Luca De Gioia and Christophe Léger, “The oxidative inactivation of FeFe hydrogenase reveals the flexibility of the H-cluster” Nature Chemistry 6, 336-342 (2014) doi:10.1038/nchem.1892 Erratum

62. V Hajj, C Baffert, K Sybirna, I Meynial-Salles, P Soucaille, H Bottin, V Fourmond, C Léger, “Reductive inactivation of FeFe hydrogenase and implication for catalysis” Energy and Environmental Science 7(2) 715-719 (2014) doi:10.1039/C3EE42075B

61. Contribution to Practical Approaches to Biological Inorganic Chemistry

60. J. Jacques Julien, V. Fourmond, P. Arnoux, M. Sabaty, E. Etienne, F. Biaso, P. Bertrand, D. Pignol, C. Léger, B. Guigliarelli, B. Burlat, “Reductive activation in periplasmic nitrate reductase involves chemical modifications of the Mo-cofactor beyond the first coordination sphere of the metal ion” BBA Bionergetics 1837 277-286 (2014) doi:10.1016/j.bbabio.2013.10.013


Structure et fonction des hydrogénases, C. Léger et S. Dementin, chapitre du livre L’énergie à découvert (2013)

59. V. Fourmond, C Baffert, K Sybirna, S Dementin, A Abou-Hamdan, I Meynial-Salles, Ph Soucaille, H Bottin, C Léger “The mechanism of inhibition by H2 of H2-evolution by hydrogenases” Chem. Commun 49, 6840-6842 (2013) doi:10.1039/C3CC43297A This was a Hot Chem Comm paper for June 2013

58. V. Fourmond, C. Baffert, K. Sybirna, T. Lautier, A. Abou Hamdan, S. Dementin, P. Soucaille, I. Meynial-Salles, H. Bottin and C. Léger, “Steady-state catalytic wave-shapes for 2-electron reversible electrocatalysts and enzymes” J. Am. Chem. Soc. 125 3926 (2013). doi:10.1021/ja311607s

57. A Abou Hamdan , B Burlat , O Gutierrez-Sanz , PP Liebgott , C Baffert , A de Lacey , M Rousset , B Guigliarelli , C Léger and S. Dementin, “O2-independent formation of the inactive states of NiFe hydrogenase” Nat. Chem. Biol. 9 15-17 (2013) doi:10.1038/NCHEMBIO.1110 M. J. Maroney (News and views) Nat. Chem. Biol (2013) doi:10.1038/nchembio.1139

56. T. Miyake, M. Bruschi, U. Cosentino, C. Baffert, V. Fourmond, C Léger, G. Moro, L. De Gioia, C. Greco. “Does the environment around the H-cluster allow coordination of the pendant amine to the catalytic iron center in [FeFe] hydrogenases? Answers from theory” J Biol Inorg Chem 18 693-700 (2013) doi:10.1007/s00775-013-1014-4

55. Kateryna Sybirna, P Ezanno, C Baffert, C Léger, H Bottin, “Arginine171 of Chlamydomonas reinhardtii FeFe hydrogenase HydA1 plays a crucial role in electron transfer to its catalytic center” Int. J. Hydrogen Energy 7 2998 2013 doi:10.1016/j.ijhydene.2012.12.078


54. A Abou Hamdan , PP Liebgott , V Fourmond , O Gutierrez-Sanz , A L De Lacey , P Infossi , M Rousset , S Dementin , C Léger, “Relation between anaerobic inactivation and oxygen tolerance in a large series of NiFe hydrogenase mutants” Proc. natl. Acad. Sc. USA 109 (49) 19916-19921 (2012) doi:10.1073/pnas.1212258109

53. C. Baffert, K. Sybirna, P. Ezanno, T. Lautier, V. Hajj, I. Meynial-Salles, P. Soucaille, H. Bottin and C. Léger, “Covalent attachment of FeFe hydrogenases to carbon electrodes for direct electron transfer”, Anal. Chem. 84 7999 (2012) doi:10.1021/ac301812s

52. A. Abou Hamdan, S. Dementin, P.-P. Liebgott, O. Gutierrez-Sanz, P. Richaud, A. L. De Lacey, M. Rousset, P. Bertrand, L. Cournac and C. Léger, “Understanding and tuning the catalytic bias of hydrogenase” J. Am. Chem. Soc. 134 8368-8371 (2012) doi:10.1021/ja301802r


51. S. Dementin, C. Burlat, V. Fourmond, F. Leroux, P.P. Liebgott, A. Abou Hamdan, C. Léger, M. Rousset, B. Guigliarelli, P. Bertrand, “Rates of intra and intermolecular electron transfers in hydrogenase deduced from steady-state activity measurements” J. Am. Chem. Soc., 133, 10211–10221 (2011) doi: 10.1021/ja202615a

50. C Baffert, L Bertini, T Lautier, C Greco, K Sybirna, P Ezanno, E Etienne, P Soucaille, P Bertrand, H Bottin, I Meynial-Salles, L De Gioia, C Léger “CO disrupts the reduced H-cluster of FeFe hydrogenase. A combined DFT and PFV study” J. Am. Chem. Soc. 133, 2096-2099 (2011) doi: 10.1021/ja110627b

49. P-P Liebgott, A L. de Lacey, B Burlat, L Cournac, P Richaud, M Brugna, V M. Fernandez, B Guigliarellia, M Rousset, C Léger, S Dementin “Original design of an oxygen-tolerant [NiFe] hydrogenase : Major effect of a valine-to-cysteine mutation near the active site” J. Am. Chem. Soc. 133, 986-997 (2011) doi:10.1021/ja108787s

48. O. Kolaj-Robin, S. R O’Kane, W. Nitschke, C. Léger, F. Baymann, T. Soulimane. “Biochemical and biophysical characterization of succinate:quinone reductase from Thermus thermophilus” BBA – Bioenergetics, 1807 68-79 (2011) doi:10.1016/j.bbabio.2010.10.009

47. T. Lautier, P. Ezanno, C. Baffert, V. Fourmond, L. Cournac, Juan C. Fontecilla-Camps, P. Soucaille, P. Bertrand, I. Meynial-Salles, Christophe Léger. “The quest for a functional substrate access tunnel in FeFe hydrogenase” Faraday Discussions, 148, 385-407 (2011). doi:10.1039/c004099c

46. P.P. liebgott, S. Dementin, C. Léger and M. Rousset “Towards engineering O2-tolerance in NiFe hydrogenases” Energy and Environmental Science 4, 33-41 (2011) doi:10.1039/c0ee00093k


45. M.E. Pandelia, V. Fourmond, P. Tron, E. Lojou, P. Bertrand, C. Léger, M.T. Giudici-Orticoni, W. Lubitz “The Membrane-Bound Hydrogenase I from the Hyperthermophilic Bacterium Aquifex aeolicus: Enzyme Activation, Redox Intermediates and Oxygen Tolerance” J. Am. Chem. Soc. 132(20) 6991-7004 (2010) doi:10.1021/ja910838d

44. V. Fourmond, P. Infossi, MT Guidici-Orticoni, P. Bertrand, C. Léger “Two-step chronoamperometric method for studying the anaerobic inactivation of an oxygen tolerant NiFe hydrogenase” J. Am. Chem. Soc. 132(13), 4848-4857 (2010) doi:10.1021/ja910685j [pdf]

43. F. Leroux, PP Liebgott, L. Cournac, P. Richaud, A. Kpebe, B. Burlat, B. Guigliarelli, P. Bertrand, C. Léger, M. Rousset, S. Dementin “Is engineering O2-tolerant hydrogenases just a matter of reproducing the active sites of the naturally occurring O2-resistant enzymes?” Int. J. H2 Energ. 35, 10770-10777 (2010) doi:10.1016/j.ijhydene.2010.02.071

42. V. Fourmond, B. Burlat, S. Dementin, M. Sabaty, P. Arnoux, E. Etienne, B. Guigliarelli, P. Bertrand, D. Pignol and C. Léger. “Dependence of catalytic activity on driving force in solution assays and protein lm voltammetry: insights from the comparison of nitrate reductase mutants” Biochemistry 49(11) 2424-2432 (2010) doi:10.1021/bi902140e [pdf]

41. V. Fourmond, M. Sabaty, P. Arnoux, P. Bertrand, D. Pignol and C. Léger. “Reassessing the Strategies for Trapping Catalytic Intermediates during Nitrate Reductase Turnover” J. Phys. Chem. B 114(9) 3341-3347 (2010) doi:10.1021/jp911443y [pdf]

40. P.-P. Liebgott, F. Leroux, B. Burlat, S. Dementin, C. Baffert, Th. Lautier, V. Fourmond, P. Ceccaldi, Ch. Cavazza, I. Meynial-Salles, Ph. Soucaille, J. Fontecilla-Camps, B. Guigliarelli, P. Bertrand, M. Rousset, Ch. Léger. “Relating diffusion along the substrate tunnel and oxygen sensitivity in hydrogenase” Nat. Chem. Biol. 6(1) 63-70 (2010) doi:10.1038/nchembio.276


39. K. H. Diêp Lê, A. Boussac, B. Frangioni, Ch. Léger, F. Lederer “Interdomain Contacts in Flavocytochrome b2, a Mutational Analysis” Biochemistry, 48, 10803-10809 (2009) doi:10.1021/bi901301r

38. S. Dementin, F. Leroux, L. Cournac, A. De Lacey, A. Volbeda, C. Léger, B. Burlat, N. Martinez, S. Champ, L. Martin, O. Sanganas, M. Haumann, V. Fernandez, B. Guigliarelli, J. Fontecilla-Camps, M. Rousset. “Introduction of Methionines in the Gas Channel Makes [NiFe] Hydrogenase Aero-Tolerant” J. Am. Chem. Soc., 131, 10156-10164 (2009) doi:10.1021/ja9018258

37. V. Fourmond, K. Hoke, H. A. Heering, C. Baffert, F. Leroux, P. Bertrand, C. Leger “SOAS: a free software to analyse electrochemical data and other one-dimensional signals” Bioelectrochemistry, 76, 141-147 (2009) doi:10.1016/j.bioelechem.2009.02.010

36. V. Fourmond, T. Lautier, C. Baffert, F. Leroux, P.-P. Liebgott, S. Dementin, M. Rousset, P. Arnoux, D. Pignol, I. Meynial, P. Soucaille, P. Bertrand, C. Léger. “Correcting for electrocatalyst desorption and inactivation in chronoamperometry experiments.” Analytical Chemistry, 81, 1962-2968 (2009) doi:10.1021/ac8025702


35. V. Fourmond, B. Burlat, S. Dementin, P. Arnoux, M. Sabaty, S. Boiry, B. Guigliarelli, P. Bertrand, D. Pignol and C. Léger “Major Mo(V) EPR signature of Rhodobacter sphaeroides periplasmic nitrate reductase arising from a dead-end species that activates upon reduction. Relation to other molybdoenzymes from the DMSO reductase family.” J. Phys. Chem. B 112, 15478-15486 (2008) doi:10.1021/jp807092y

34. F. Leroux, S. Dementin, B. Burlat, L. Cournac, A. Volbeda, S. Champ, L. Martin, B. Guigliarelli, P. Bertrand, J. Fontecilla-Camps, M. Rousset and C. Léger “Experimental Approaches to Kinetics of Gas Diffusion in Hydrogenase” Proc. Natl. Acad. Sci. USA 105, 11188 (2008) doi:10.1073/pnas.0803689105

33. C. Léger and P. Bertrand. “Direct electrochemistry of redox enzymes as a tool for mechanistic studies” Chem. Rev. 108, 2379 (2008) (open access) doi:10.1021/cr0680742 This is part of the July, special issue on Molecular and biomolecular electrochemistry

32. C. Baffert, M. Demuez, L. Cournac, B. Burlat, B. Guigliarelli, P. Bertrand, L. Girbal and C. Léger. “Hydrogen-activating enzymes: activity does not correlate with oxygen sensitivity” Angewandte Chemie Int. Ed. 47, 2052 (2008) doi:10.1002/anie.200704313


31. O. Guerrini, B. Burlat B, C. Léger, B. Guigliarelli, P. Soucaille, L. Girbal “Characte- rization of two 2[4Fe4S] ferredoxins from Clostridium acetobutylicum” Curr Microbiol. 56, 261-267 (2008).

30. P. Bertrand, B. Frangioni, S. Dementin, M. Sabaty, P. Arnoux, B. Guigliarelli, D. Pignol and C. Léger. « Effects of slow substrate binding and release in redox enzymes: theory and application to periplasmic nitrate reductase.’’ J. Phys. Chem. B 111, 10300 (2007). doi:10.1021/jp074340j

29. S. Dementin, P. Arnoux, B. Frangioni, S. Grosse, C. Léger, B. Burlat, B. Guigliarelli, M. Sabaty, D. Pignol. “Access to the Active Site of Periplasmic Nitrate Reductase: Insights from Site-Directed Mutagenesis and Zinc Inhibition Studies” Biochemistry 38, 12240 (2007) doi:10.1021/bi700928m

28. M. G. Almeida, Celia M. Silveira, B. Guigliarelli, P. Bertrand, J. J. G. Moura, I. Moura and C. Léger. “A needle in a haystack: the active site of the membrane-bound complex cytochrome c nitrite reductase.” FEBS Letters 581, 284 (2007). doi:10.1016/j.febslet.2006.12.023


27. S. Dementin, V. Belle, P. Bertrand, B. Guigliarelli, G. Adryanczyk-Perrier, A. Delacey, V. M. Fernandez, M. Rousset and C. Léger. “Changing the ligation of the distal [4Fe4S] cluster in NiFe hydrogenase impairs inter- and intramolecular electron transfers” J. Am. Chem. Soc. 128, 5209 (2006) doi:10.1021/ja060233b

26. C. Léger, F. Lederer, B. Guigliarelli and P. Pertrand, “Electron flow in multicenter enzymes: theory, applications and consequences on the natural design of redox chains” J. Am. Chem. Soc. 128, 180 (2006) doi:10.1021/ja055275z

25. M. Guiral, P. Tron, V. Belle, C. Aubert, C. Léger, B. Guigliarelli and M.-T. Giudici-Orticoni. “Hyperthermostable and oxygen resistant hydrogenases from a hyperthermophilic bacterium Aquifex aeolicus: Physicochemical properties” Int. J. Hydrogen. Energ. 31, 1414 (2006) doi:10.1016/j.ijhydene.2006.06.007


24. C. Léger, S. Dementin, P. Bertrand, M. Rousset and B. Guigliarelli, “Inhibition and aerobic inactivation kinetics of Desulfovibrio fructosovorans NiFe hydrogenase studied by Protein Film voltammetry” J. Am. Chem. Soc. 126, 12162 (2004) doi:10.1021/ja046548d

23. B. Frangioni, P. Arnoux, M. Sabaty, D. Pignol, P. Bertrand, B. Guigliarelli and C. Léger “In Rhodobacter sphaeroides respiratory nitrate reductase, the kinetics of substrate binding favors intramolecular electron transfer” J. Am. Chem. Soc., 126, 1328 (2004) doi:10.1021/ja0384072


22. C. Léger, S. J. Elliott, K. J. Hoke, L. J. C. Jeuken, A. K. Jones, and F. A. Armstrong. “Enzyme electrokinetics: using protein film voltammetry to investigate redox enzymes and their mechanisms,” Biochemistry, Current Topics 42-29, 8653-8662 (2003). doi:10.1021/bi034789c

21. V. Yankovskaya, R. Horsefield, S. Tornroth, C. Luna-Chavez, H. Miyoshi, C Léger, B. Byrne, G. Cecchini and S. Iwata, “Molecular architecture of succinate dehydrogenase (Complex II) prevents reactive oxygen species generation,” Science, 299 700-704 (2003). doi:10.1126/science.1079605


20. C. Léger, A. K. Jones, W. Roseboom, S. P. J. Albracht and F. A. Armstrong “Enzyme electrokinetics: hydrogen evolution and oxydation by A. vinosum [Ni-Fe]-hydrogenase,” Biochemistry, 41-52, 15736-15746 (2002). doi:10.1021/bi026586e

19. C. Léger, A. K. Jones, S. P. J. Albracht and F. A. Armstrong, “Effect of a dispersion of interfacial electron transfer rates on steady state catalytic electron transport in [Ni-Fe]-hydrogenase and other enzymes,” J. Phys. Chem. B, 106-50, 13058-13063 (2002). doi:10.1021/jp0265687

18. S. J. Elliott, C. Léger, H. R. Pershad, J. Hirst, K. Heffron, F. Blasco, R. A. Rothery, J. W. Weiner and F. A. Armstrong, “Detection and interpretation of redox potential optima in the catalytic activity of enzymes,” Biochim. Biophys. Acta (Bioenergetics), 1555-1/3, 54-59 (2002) doi:10.1016/S0005-2728(02)00254-2


17. L. Bateman, C. Léger, D. B. Goodin and F. A. Armstrong, “A distal histidine mutant (H52Q) of yeast cytochrome c Peroxidase catalyses the oxidation of H~2~O~2~ instead of its reduction,” J. Am. Chem. Soc., 123-38, 9260-9263 (2001). doi:10.1021/ja0158612

16. C. Léger, K. Heffron, H. Pershad, E. Maklashina, C. Luna-Chavez, G. Cecchini, B. A. C. Ackrell and F. A. Armstrong, “Enzyme electrokinetics: energetics of succinate oxidation by fumarate reductase and succinate dehydrogenase,” Biochemistry 40-37, 11234-11245 (2001) doi:10.1021/bi010889b

15. K. Heffron, C. Léger, R. A. Rothery, J. H. Weiner and F. A. Armstrong, “Determination of an optimal potential window for catalysis by E. Coli dimethyl sulfoxide reductase, and hypothesis on the role of MoV in the reaction pathway,” Biochemistry, 40-10, 3117-3126 (2001). doi:10.1021/bi002452u


14. F. A. Armstrong, R. Camba, H. A. Heering, J. Hirst, L. J. C. Jeuken, A. K. Jones, C. Léger and J. P. McEvoy, “Fast voltammetric studies of the kinetics and energetics of coupled electron-transfer reactions in proteins,” Faraday Discuss., 116 (2000). doi:10.1039/b002290j

13. C. H. Chen, C. A. Miller, J. M. Walsh, P. B. Warren, J. N. Ruddock, P. R. Garrett, F. Argoul and C. Léger, “Dissolution rates of pure nonionic surlactants,” Langmuir 16-12, 5276-5283 (2000). doi:10.1021/la9913497

12. C. Léger, J. Elezgaray and F. Argoul, “Internal structure of dense electrodeposits,” Phys. Rev. E. 61-5, 5452-5463 (2000). doi:10.1103/PhysRevE.61.5452

11. J. Elezgaray, C. Léger and F. Argoul, “Dense branching morphology in electrodeposition experiments: characterization and mean-field modeling,” Phys. Rev. Lett. 84-14, 3129-3132 (2000). doi:10.1103/PhysRevLett.84.3129

10. C. Léger, J. Elezgaray and F. Argoul, “Probing interfacial dynamics by phase-shift interferometry in thin cell electrodeposition,” J. Electroanal. Chem. 486, 204-219 (2000). doi:10.1016/S0022-0728(00)00143-1


9. C. Léger et C. Delmas, “L’electrode positive d’hydroxyde de nickel pour batteries alcalines,” Bulletin de l’Union des Physiciens 93-811, 291-301 (1999).

8. C. Léger, C. Tessier, M. Menetrier, C. Denage and C. Delmas, “Investigations of the second discharge plateau of the betta(III)-NiOOH/beta(II)-Ni(OH)2 system,” J. Electrochem. Soc. 146-3, 924-932 (1999).

7. C. Léger, L. Servant, J.-L. Bruneel and F. Argoul, “Growth patterns in electrodeposition,” Physica A 263(1-4), 305-314 (1999).

6. C. Léger, F. Argoul and M. Z. Bazant, » “Front dynamics during diffusion-limited corrosion of ramified electrodeposits,” J. Phys. Chem. B 103-28, 5841-5851 (1999). doi:10.1021/jp990486+


5. C. Léger, J. Elezgaray and F. Argoul, “Dynamical characterization of one dimensional stationary growth regimes in diffusion-limited electrodeposition processes,” Phys. Rev. E 58-6, 7700-7709 (1998).

4. J. Elezgaray, C. Léger and F. Argoul, “Linear stability analysis of unsteady galvano- static electrodeposition in the 2D diffusion limited regime,” J. Electrochem. Soc. 145-6, 2016-2024 (1998).


3. F. Texier, G. Gadret, C. Léger and F. Argoul, “Convection induced self-organization in electroless deposition experiments,” J. Phys. II France 7, 663-675 (1997).

2. C. Léger, J. Elezgaray and F. Argoul, “Experimental demonstration of diffusion-limited dynamics in electrodeposition experiments,” Phys. Rev. Lett. 78-26, 5010-5013 (1997).


1. F. Argoul, E. Freysz, A. Kuhn, C. Léger and L. Potin, “Interferometric characterization of growh dynamics during dendritic electrodeposition of zinc,” Phys. Rev. E. 53, 1777-1787 (1996)