Enzymes à molybdène et métabolismes associés

Molybdenum enzymes and associated metabolism



Maryam Seif Eddine, Frédéric Biaso, Julia Rendon, Eric Pilet, Bruno Guigliarelli, Axel Magalon, Stéphane Grimaldi.
1,2H hyperfine spectroscopy and DFT modeling unveil the demethylmenasemiquinone binding mode to E. coli nitrate reductase A (NarGHI).
Biochimica et Biophysica Acta (BBA) – Bioenergetics, 2020. DOI: 10.1016/j.bbabio.2020.148203

Ahmed Djeghader, Mélanie Rossotti, Saleh Abdulkarim, Frédéric Biaso, Guillaume Gerbaud, Wolfgang Nitschke, Barbara Schoepp-Cothenet, Tewfik Soulimane, Stephane Grimaldi.
Structural evidence for a reaction intermediate mimic in the active site of a sulfite dehydrogenase.
Chem. Commun., 2020. DOI: 10.1039/D0CC03634J


Arkadiusz Zupok, Chantal Iobbi-Nivol, Vincent Méjean, Silke Leimkühler.
The regulation of Moco biosynthesis and molybdoenzyme gene expression by molybdenum and iron in bacteria.
Metallomics, 2019, 11 (10), 1602 – 1624. DOI: 10.1039/c9mt00186g HAL: hal-02372050v1

Biljana Mitrova, Armel F. T. Waffo, Paul Kaufmann, Chantal Iobbi‐Nivol, Silke Leimkühler, Ulla Wollenberger.
Trimethylamine N ‐Oxide Electrochemical Biosensor with a Chimeric Enzyme.
ChemElectroChem, 2019, 6 (6), 141 – 1737. DOI: 10.1002/celc.201801422 HAL: hal-02273149v1


Paul Kaufmann, Benjamin R. Duffus, Biljana Mitrova, Chantal Iobbi-Nivol, Christian Teutloff, Manfred Nimtz, Lothar Jänsch, Ulla Wollenberger, Silke Leimkühler.
Modulating the Molybdenum Coordination Sphere of Escherichia coli Trimethylamine N -Oxide Reductase.
Biochemistry, 2018, 57 (7), 1130 – 1143. DOI: 10.1021/acs.biochem.7b01108 HAL: hal-01889976v1

Nadine Schwanhold, Chantal Iobbi-Nivol, Angelika Lehmann, Silke Leimkühler.
Same but different: Comparison of two system-specific molecular chaperones for the maturation of formate dehydrogenases.
PLoS ONE, 2018, 4 (4), 406 –. DOI: 10.1371/journal.pone.0201935 HAL: hal-01927954v1


Julia Rendon, Frédéric Biaso, Pierre Ceccaldi, René Toci, Farida Seduk, Axel Magalon, Bruno Guigliarelli, Stéphane Grimaldi.
Elucidating the Structures of the Low- and High-pH Mo(V) Species in Respiratory Nitrate Reductase: A Combined EPR, 14,15 N HYSCORE, and DFT Study.
Inorg. Chem., 2017, 56 (8), 4422 – 4434. DOI: 10.1021/acs.inorgchem.6b03129 HAL: hal-01514650v1

Maryam Seif Eddine, Frédéric Biaso, Rodrigo Arias‐Cartin, Eric Pilet, Julia Rendon, Sevdalina Lyubenova, Farida Seduk, Bruno Guigliarelli, Axel Magalon, Stéphane Grimaldi.
Probing the Menasemiquinone Binding Mode to Nitrate Reductase A by Selective 2 H and 15 N Labeling, HYSCORE Spectroscopy, and DFT Modeling.
ChemPhysChem, 2017, 45 (19), 287 – 2714. DOI: 10.1002/cphc.201700571 HAL: hal-01635739v1


Olivier N. Lemaire, Flora A. Honoré, Cécile Jourlin-Castelli, Vincent Méjean, Michel Fons, Chantal Iobbi-Nivol.
Efficient respiration on TMAO requires TorD and TorE auxiliary proteins in Shewanella oneidensis.
Research in Microbiology, 2016, 167 (8), 630 – 637. DOI: 10.1016/j.resmic.2016.05.004 HAL: hal-01411703v1

Stéphane Grimaldi, Frédéric Biaso, Bénédicte Burlat, Bruno Guigliarelli.
Electron paramagnetic resonance studies of molybdenum enzymes.
Molybdenum and Tungsten Enzymes : Spectroscopic and Theoretical Investigations. RSC Metallobiology Series. Editors: Russ Hille, Carola Schulzke, Martin L Kirk, 2016, 68 – 120. DOI: 10.1039/9781782628842-00068 HAL: hal-01441142v1

Silke Leimkühler, Olivier N Lemaire, Chantal Iobbi-Nivol.
2016, 117 – 142. DOI: 10.1039/9781782623915-00117 HAL: hal-01446287v1

Rodrigo Arias-Cartin, Pierre Ceccaldi, Barbara Schoepp-Cothenet, Klaudia Frick, Jean-Michel Blanc, Bruno Guigliarelli, Anne Walburger, Stéphane Grimaldi, Thorsten Friedrich, Véronique Receveur-Brechot, Axel Magalon.
Redox cofactors insertion in prokaryotic molybdoenzymes occurs via a conserved folding mechanism.
Sci Rep, 2016, 12 (1), 543 –. DOI: 10.1038/srep37743 HAL: hal-01415067v1

Simon Duval, Joanne M. Santini, David Lemaire, Florence Chaspoul, Michael J. Russell, Stephane Grimaldi, Wolfgang Nitschke, Barbara Schoepp-Cothenet.
The H-bond network surrounding the pyranopterins modulates redox cooperativity in the molybdenum- bis PGD cofactor in arsenite oxidase.
Biochimica et Biophysica Acta (BBA) – Bioenergetics, 2016, 1857 (9), 1353 – 1362. DOI: 10.1016/j.bbabio.2016.05.003 HAL: hal-01413292v1


Silke Leimkühler, Chantal Iobbi-Nivol.
Bacterial molybdoenzymes: old enzymes for new purposes.
FEMS Microbiology Reviews, 2015, 1853 (1), 1335 – 18. DOI: 10.1093/femsre/fuv043 HAL: hal-01413145v1

Julia Rendon, Eric Pilet, Zeinab Fahs, Farida Seduk, Léa Sylvi, Mahmoud Hajj Chehade, Fabien Pierrel, Bruno Guigliarelli, Axel Magalon, Stephane Grimaldi.
Demethylmenaquinol is a substrate of Escherichia coli nitrate reductase A (NarGHI) and forms a stable semiquinone intermediate at the NarGHI quinol oxidation site.
Biochimica et Biophysica Acta (BBA) – Bioenergetics, 2015, 1847 (8), 739 – 747. DOI: 10.1016/j.bbabio.2015.05.001 HAL: hal-01429032v1

Pierre Ceccaldi, Julia Rendon, Christophe Léger, René Toci, Bruno Guigliarelli, Axel Magalon, Stéphane Grimaldi, Vincent Fourmond.
Reductive activation of E. coli respiratory nitrate reductase.
Biochimica et Biophysica Acta (BBA) – Bioenergetics, 2015, 1847 (10), 1055 – 1063. DOI: 10.1016/j.bbabio.2015.06.007 HAL: hal-01429839v1


Stéphane Grimaldi, Barbara Schoepp-Cothenet, Pierre Ceccaldi, Bruno Guigliarelli, Axel Magalon.
The prokaryotic Mo/W-bisPGD enzymes family: A catalytic workhorse in bioenergetic.
Biochimica et Biophysica Acta (BBA) – Bioenergetics, 2013, 1827 (8-9), 1048 – 1085. DOI: 10.1016/j.bbabio.2013.01.011


Sébastien Dementin, Pascal Arnoux, Bettina Frangioni, Sandrine Grosse, Christophe Léger, Bénédicte Burlat, Bruno Guigliarelli, Monique Sabaty, David Pignol.
Access to the Active Site of Periplasmic Nitrate Reductase:  Insights from Site-Directed Mutagenesis and Zinc Inhibition Studies.
Biochemistry, 2007, 46 (34), 9713 – 9721. DOI: 10.1021/bi700928m HAL: hal-00336040


E. Lebrun, M. Brugna, F. Baymann, D. Muller, D. Lievremont, M.-C. Lett, W. Nitschke.
Arsenite Oxidase, an Ancient Bioenergetic Enzyme.
2003, 20 (5), 686 – 693. DOI: 10.1093/molbev/msg071 HAL: hal-00113712v1