Corrigendum to 'Transport limited adsorption experiments give a new lower estimate of the turnover frequency of Escherichia coli hydrogenase 1' BBA Advances 3 (2023) 100090

Autor: Anna Aldinio-Colbachini, Andrea Fasano, Chloé Guendon, Aurore Jacq-Bailly, Jérémy Wozniak, Carole Baffert, Arlette Kpebe, Christophe Léger, Myriam Brugna, Vincent Fourmond

Publikováno v: BBA Advances, Vol 5, Iss , Pp 100116- (2024)

Externí odkaz: https://doaj.org/article/6cc8649744224b96b86c2be22df7b8a0

A safety cap protects hydrogenase from oxygen attack

Autor: 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

Publikováno v: Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)

[FeFe]-hydrogenases catalyze the conversion of protons and electrons to molecular hydrogen, but upon exposure to oxygen, their catalytic cofactor is irreversibly inactivated. Here, the authors determine the crystal structure of hydrogenase CbA5H and

Externí odkaz: https://doaj.org/article/9c9745d6547b4e9c8c0781318c4c1e61

Assessing the Extent of Potential Inversion by Cyclic Voltammetry: Theory, Pitfalls, and Application to a Nickel Complex with Redox-Active Iminosemiquinone Ligands

Autor: Cheriehan Hessin, Jules Schleinitz, Nolwenn Le Breton, Sylvie Choua, Laurence Grimaud, Vincent Fourmond, Marine Desage-El Murr, Christophe Léger

Publikováno v: Inorganic Chemistry
Inorganic Chemistry, 2023, 62 (8), pp.3321-3332. ⟨10.1021/acs.inorgchem.2c04365⟩

International audience; Potential inversion refers to the situation where a protein cofactor or a synthetic molecule can be oxidized or reduced twice in a cooperative manner, that is the second electron transfer (ET) is easier than the first. This pr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11a3248c2d5b9259ce245c5e2b8a256c
https://doi.org/10.1021/acs.inorgchem.2c04365

Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase

Autor: Elizabeth C Wittenborn, Mériem Merrouch, Chie Ueda, Laura Fradale, Christophe Léger, Vincent Fourmond, Maria-Eirini Pandelia, Sébastien Dementin, Catherine L Drennan

Publikováno v: eLife, Vol 7 (2018)

The C-cluster of the enzyme carbon monoxide dehydrogenase (CODH) is a structurally distinctive Ni-Fe-S cluster employed to catalyze the reduction of CO2 to CO as part of the Wood-Ljungdahl carbon fixation pathway. Using X-ray crystallography, we have

Externí odkaz: https://doaj.org/article/6a9fdef703824e8a8dbe1dc0311b6bd7

Formate Dehydrogenases Reduce CO 2 Rather than HCO 3 − : An Electrochemical Demonstration

Autor: Marta Meneghello, Inês A. C. Pereira, Ana Rita Oliveira, Vincent Fourmond, Christophe Léger, Aurore Jacq-Bailly

Publikováno v: Angewandte Chemie International Edition
Angewandte Chemie International Edition, 2021, ⟨10.1002/anie.202101167⟩
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2021, ⟨10.1002/anie.202101167⟩
Angew Chem Int

International audience; Mo/W formate dehydrogenases catalyze the reversible reduction of CO 2 species to formate. It is thought that the substrate is CO 2 and not a hydrated species like HCO-3 , but there is still no indisputable evidence for this, i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::805b449fad5f62d9a97b968536886ec6
https://doi.org/10.1002/ange.202101167