Pierre Ceccaldi
Uppsala University
15 Papers
91 Citations
Pierre Ceccaldi is an academic researcher from Uppsala University. The author has contributed to research in topics: Hydrogenase & Chemistry. The author has an hindex of 11, co-authored 15 publications. Previous affiliations of Pierre Ceccaldi include Boston University & Centre national de la recherche scientifique.
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Papers
Relating diffusion along the substrate tunnel and oxygen sensitivity in hydrogenase
Pierre-Pol Liebgott,Fanny Leroux,Fanny Leroux,Bénédicte Burlat,Bénédicte Burlat,Sébastien Dementin,Carole Baffert,Carole Baffert,Thomas Lautier,Thomas Lautier,Vincent Fourmond,Pierre Ceccaldi,Pierre Ceccaldi,Christine Cavazza,Isabelle Meynial-Salles,Isabelle Meynial-Salles,Philippe Soucaille,Juan C. Fontecilla-Camps,Bruno Guigliarelli,Bruno Guigliarelli,Patrick Bertrand,Patrick Bertrand,Marc Rousset,Christophe Léger +23 more
TL;DR: It is demonstrated that certain enzymes are slowly inactivated by O2 because access to the active site is slow, and the relations between diffusion, the Michaelis constant for H2 and rates of inhibition are quantitatively defined.
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Spectroscopic investigations under whole-cell conditions provide new insight into the metal hydride chemistry of [FeFe]-hydrogenase
Lívia S. Mészáros,Pierre Ceccaldi,Marco Lorenzi,Holly J. Redman,Emanuel Pfitzner,Joachim Heberle,Moritz Senger,Sven T. Stripp,Gustav Berggren +8 more
TL;DR: Through a combination of gas treatments, pH titrations, and isotope editing, a number of proposed catalytic intermediates in living cells are corroborated, supporting their physiological relevance and a previously incompletely characterized catalytic intermediate is reported herein.
The hydrogen dependent CO2 reductase: the first completely CO tolerant FeFe-hydrogenase
TL;DR: In this article, the electrocatalytic properties of the hydrogenase (Hase) module in the intact complex, including (an)aerobic oxidation, CO inhibition and the first systematic analysis of the catalytic bias (CB) of a Hase.
In Vivo EPR Characterization of Semi-Synthetic [FeFe] Hydrogenases.
TL;DR: The study provides the first spectroscopic characterization of semi‐synthetic hydrogenases in’vivo, and the observation of two different oxidized states of the H‐cluster under intracellular conditions underscore how synthetic chemistry can be a powerful tool for manipulation and examination of the hydrogenase enzyme under in vivo conditions.
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Oxidative inactivation of NiFeSe hydrogenase
TL;DR: A resolution to the paradox that spectroscopic studies of NiFeSe hydrogenase have not revealed any major signal attributable to Ni(III) states formed upon reaction with O2, despite the fact that two inactive states are formed upon either aerobic or anaerobic oxidation is proposed.
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