Life with Carbon Monoxide, Crit. Rev. Biochem. Mol. Biol, vol.39, issue.3, pp.165-195, 2004. ,
Anaerobic Growth of a Rhodopseudomonas Species in the Dark with Carbon Monoxide as Sole Carbon and Energy Substrate, Proc. Natl. Acad. Sci. U. S. A, vol.73, issue.9, pp.3298-3302, 1976. ,
Life on Carbon Monoxide: X-Ray Structure of Rhodospirillum rubrum Ni-Fe-S Carbon Monoxide Dehydrogenase, Proceedings of the National Academy of Sciences, issue.21, pp.11973-11978, 2001. ,
Crystal Structure of a Carbon Monoxide Dehydrogenase Reveals a [Ni-4Fe-5S] Cluster, Science, vol.293, issue.5533, pp.1281-1285, 2001. ,
Kinetic Evidence That Carbon Monoxide Dehydrogenase Catalyzes the Oxidation of Carbon Monoxide and the Synthesis of Acetyl-CoA at Separate Metal Clusters, J. Am. Chem. Soc, vol.115, issue.24, pp.11646-11647, 1993. ,
Organization of Clusters and Internal Electron Pathways in CO Dehydrogenase from Clostridium thermoaceticum : Relevance to the Mechanism of Catalysis and Cyanide Inhibition, Biochemistry, vol.33, issue.29, pp.8702-8711, 1994. ,
Redox-Dependent Rearrangements of the NiFeS Cluster of Carbon Monoxide Dehydrogenase, vol.7, p.39451, 2018. ,
URL : https://hal.archives-ouvertes.fr/hal-01917213
CODH-IV: A High-Efficiency CO-Scavenging CO Dehydrogenase with Resistance to O 2, Angew. Chem. Int. Ed Engl, vol.2017, issue.48, pp.15466-15469 ,
URL : https://hal.archives-ouvertes.fr/hal-01696167
Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] Clusters in Closed and Open Subunits of Acetyl-CoA Synthase/carbon Monoxide Dehydrogenase, Nat. Struct. Biol, vol.10, issue.4, pp.271-279, 2003. ,
A Ni-Fe-Cu Center in a Bifunctional Carbon Monoxide Dehydrogenase/acetyl-CoA Synthase, Science, vol.298, issue.5593, pp.567-572, 2002. ,
Activation of the Nickel-Deficient Carbon Monoxide Dehydrogenase from Rhodospirillum rubrum : Kinetic Characterization and Reductant Requirement, Biochemistry, vol.29, issue.8, pp.2162-2168, 1990. ,
Membrane-Associated NiFeS-Carbon Monoxide Dehydrogenases from the Anaerobic Carbon-Monoxide-Utilizing Eubacterium Carboxydothermus hydrogenoformans, J. Bacteriol, vol.183, issue.17, pp.5134-5144, 2001. ,
Properties of Purified Carbon Monoxide Dehydrogenase from Clostridium thermoaceticum , a Nickel, Iron-Sulfur Protein, J. Biol. Chem, vol.258, issue.4, pp.2364-2369, 1983. ,
The Carbon Monoxide Dehydrogenase from Desulfovibrio vulgaris, Biochim. Biophys. Acta, issue.12, pp.1574-1583, 2015. ,
O 2 Inhibition of Ni-Containing CO Dehydrogenase Is Partly Reversible, Chemistry, vol.21, issue.52, pp.18934-18938, 2015. ,
URL : https://hal.archives-ouvertes.fr/hal-01432205
O 2 -Independent Formation of the Inactive States of NiFe Hydrogenase, Nat. Chem. Biol, vol.2013, issue.1, pp.15-17 ,
URL : https://hal.archives-ouvertes.fr/hal-01977594
Investigations by Protein Film Electrochemistry of Alternative Reactions of Nickel-Containing Carbon Monoxide Dehydrogenase, J. Phys. Chem. B, issue.43, pp.13690-13697, 2015. ,
The Two CO-Dehydrogenases of Thermococcus Sp. AM4, Biochim. Biophys. Acta Bioenerg, 2020. ,
URL : https://hal.archives-ouvertes.fr/hal-02537797
Electrochemical Investigations of Hydrogenases and Other Enzymes That Produce and Use Solar Fuels, Acc. Chem. Res, vol.51, issue.3, pp.769-777, 2018. ,
URL : https://hal.archives-ouvertes.fr/hal-01745738
Pathways of Oxidative Damage, Annu. Rev. Microbiol, vol.57, pp.395-418, 2003. ,
Iron-Sulphur Clusters and the Problem with Oxygen, Mol. Microbiol, vol.59, issue.4, pp.1073-1082, 2006. ,
Iron-Sulfur Clusters: Nature's Modular, Multipurpose Structures, Science, vol.277, issue.5326, pp.653-659, 1997. ,
Mechanism of O 2 Diffusion and Reduction in FeFe Hydrogenases, Nat. Chem, vol.2017, issue.1, pp.88-95 ,
Loss of Specific Active-Site Iron Atoms in Oxygen-Exposed [FeFe]-Hydrogenase Determined by Detailed X-Ray Structure Analyses, J. Am. Chem. Soc, issue.44, pp.17721-17728, 2019. ,
FeFe]-Hydrogenase Oxygen Inactivation Is Initiated at the H Cluster 2Fe Subcluster, J. Am. Chem. Soc, vol.137, issue.5, pp.1809-1816, 2015. ,
O 2 -Tolerant, Hydrogenases of Ralstonia eutropha H16: Physiology, Molecular Biology, Purification, and Biochemical Analysis, vol.613, pp.117-151, 2018. ,
URL : https://hal.archives-ouvertes.fr/hal-02344331
Suppressing Hydrogen Peroxide Generation to Achieve Oxygen-Insensitivity of a [NiFe] Hydrogenase in Redox Active Films, Nat. Commun, vol.2020, issue.1, p.920 ,
Engineering an [FeFe]-Hydrogenase: Do Accessory Clusters Influence O 2 Resistance and Catalytic Bias?, J. Am. Chem. Soc, issue.16, pp.5516-5526, 2018. ,
URL : https://hal.archives-ouvertes.fr/hal-01759288
Structural Conversions of Synthetic and Protein-Bound Iron-Sulfur Clusters, Chem. Rev, vol.116, issue.22, pp.13685-13713, 2016. ,
Structural Insight into Metallocofactor Maturation in Carbon Monoxide Dehydrogenase, J. Biol. Chem, vol.294, issue.35, pp.13017-13026, 2019. ,
URL : https://hal.archives-ouvertes.fr/hal-02188452
Rates of Intra-and Intermolecular Electron Transfers in Hydrogenase Deduced from Steady-State Activity Measurements, J. Am. Chem. Soc, issue.26, pp.10211-10221, 2011. ,
URL : https://hal.archives-ouvertes.fr/hal-00677402
Structural and Phylogenetic Diversity of Anaerobic Carbon-Monoxide Dehydrogenases, Front. Microbiol, vol.9, p.3353, 2018. ,
The Genome Sequence of the Anaerobic, Sulfate-Reducing Bacterium Desulfovibrio vulgaris Hildenborough, Nat. Biotechnol, vol.22, issue.5, pp.554-559, 2004. ,
Growth of the Obligate Anaerobe Desulfovibrio vulgaris Hildenborough under Continuous Low Oxygen Concentration Sparging: Impact of the Membrane-Bound Oxygen Reductases, PLoS One, vol.10, issue.4, p.123455, 2015. ,
URL : https://hal.archives-ouvertes.fr/hal-01216176
, Acta Crystallogr. D Biol. Crystallogr, issue.2, pp.125-132, 2010.
Phaser Crystallographic Software, J. Appl. Crystallogr, pp.658-674, 2007. ,
A Comprehensive Python-Based System for Macromolecular Structure Solution, Acta Crystallogr. D Biol. Crystallogr, pp.213-221, 2010. ,
Features and Development of Coot, Acta Crystallogr. D Biol. Crystallogr, pp.486-501, 2010. ,
Optimal Description of a Protein Structure in Terms of Multiple Groups Undergoing TLS Motion, Acta Crystallogr. D Biol. Crystallogr, vol.62, pp.439-450, 2006. ,
MolProbity: All-Atom Structure Validation for Macromolecular Crystallography, Acta Crystallogr. D Biol. Crystallogr, pp.12-21, 2010. ,
The PyMOL Molecular Graphics System, Version 1.8, 2015. ,
Collaboration Gets the Most out of Software, 1456. ,