S. Grimaldi

发表

Direct Evidence for Nitrogen Ligation to the High Stability Semiquinone Intermediate in Escherichia coli Nitrate Reductase A*

B. Guigliarelli, A. Magalon, T. Prisner, 2009, The Journal of Biological Chemistry.

Crystallographic snapshots of a B12-dependent radical SAM methyltransferase

L. Chavas, Pierre Legrand, A. Guillot, 2022, Nature.

Identification and characterization of a noncanonical menaquinone-linked formate dehydrogenase

R. Lebrun, G. Gerbaud, A. Walburger, 2021, The Journal of biological chemistry.

Reductive activation of E. coli respiratory nitrate reductase.

B. Guigliarelli, A. Magalon, C. Léger, 2015, Biochimica et biophysica acta.

Intermediate in Escherichia coli Nitrate of High Stability Menasemiquinone Determination of the Proton Environment Bioenergetics

B. Guigliarelli, A. Magalon, T. Prisner, 2013 .

Determination of the Proton Environment of High Stability Menasemiquinone Intermediate in Escherichia coli Nitrate Reductase A by Pulsed EPR*

B. Guigliarelli, A. Magalon, T. Prisner, 2011, The Journal of Biological Chemistry.

HYSCORE evidence that endogenous mena- and ubisemiquinone bind at the same Q site (Q(D)) of Escherichia coli nitrate reductase A.

B. Guigliarelli, A. Magalon, T. Prisner, 2010, Journal of the American Chemical Society.

The H-bond network surrounding the pyranopterins modulates redox cooperativity in the molybdenum-bisPGD cofactor in arsenite oxidase.

M. Russell, B. Schoepp‐Cothenet, S. Duval, 2016, Biochimica et biophysica acta.

The prokaryotic Mo/W-bisPGD enzymes family: a catalytic workhorse in bioenergetic.

B. Guigliarelli, A. Magalon, B. Schoepp‐Cothenet, 2013, Biochimica et biophysica acta.

Structural evidence for a reaction intermediate mimic in the active site of a sulfite dehydrogenase.

G. Gerbaud, A. Djeghader, T. Soulimane, 2020, Chemical communications.

Elucidating the Structures of the Low- and High-pH Mo(V) Species in Respiratory Nitrate Reductase: A Combined EPR, 14,15N HYSCORE, and DFT Study.

B. Guigliarelli, A. Magalon, P. Ceccaldi, 2017, Inorganic chemistry.

Gating of Substrate Access and Long-Range Proton Transfer in Escherichia coli Nitrate Reductase A: The Essential Role of a Remote Glutamate Residue

B. Guigliarelli, A. Magalon, Sinan Al-Attar, 2021, ACS Catalysis.

Demethylmenaquinol is a substrate of Escherichia coli nitrate reductase A (NarGHI) and forms a stable semiquinone intermediate at the NarGHI quinol oxidation site.

B. Guigliarelli, A. Magalon, F. Pierrel, 2015, Biochimica et biophysica acta.

Cardiolipin-based respiratory complex activation in bacteria

G. Giordano, B. Guigliarelli, A. Magalon, 2011, Proceedings of the National Academy of Sciences.

1,2H hyperfine spectroscopy and DFT modeling unveil the demethylmenasemiquinone binding mode to E. coli nitrate reductase A (NarGHI).

B. Guigliarelli, A. Magalon, S. Grimaldi, 2020, Biochimica et biophysica acta. Bioenergetics.

Probing the Menasemiquinone Binding Mode to Nitrate Reductase A by Selective 2 H and 15 N Labeling, HYSCORE Spectroscopy, and DFT Modeling.

B. Guigliarelli, A. Magalon, S. Grimaldi, 2017, Chemphyschem : a European journal of chemical physics and physical chemistry.

Elucidating mechanisms in haem copper oxidases: the high-affinity QH binding site in quinol oxidase as studied by DONUT-HYSCORE spectroscopy and density functional theory.

H. Michel, S. Kacprzak, M. Kaupp, 2011, Faraday discussions.

Cardiolipin binding in bacterial respiratory complexes: structural and functional implications.

B. Guigliarelli, A. Magalon, P. Arnoux, 2012, Biochimica et biophysica acta.

New method for the spin quantitation of [4Fe-4S](+) clusters with S = (3)/(2). Application to the FS0 center of the NarGHI nitrate reductase from Escherichia coli.

B. Guigliarelli, A. Magalon, P. Bertrand, 2007, The journal of physical chemistry. B.

Mutations in Both Sides of the Photosystem I Reaction Center Identify the Phylloquinone Observed by Electron Paramagnetic Resonance Spectroscopy*

Feifei Gu, R. Bittl, K. Redding, 2001, The Journal of Biological Chemistry.

Asymmetric binding of the high-affinity Q(H)(*)(-) ubisemiquinone in quinol oxidase (bo3) from Escherichia coli studied by multifrequency electron paramagnetic resonance spectroscopy.

H. Michel, H. Miyoshi, T. Mogi, 2003, Biochemistry.

QH*- ubisemiquinone radical in the bo3-type ubiquinol oxidase studied by pulsed electron paramagnetic resonance and hyperfine sublevel correlation spectroscopy.

H. Michel, B. Ludwig, T. Prisner, 2001, Biochemistry.

Crystallographic snapshots of a B12-dependent radical SAM methyltransferase

L. Chavas, Pierre Legrand, A. Guillot, 2022, Nature.

Classification of PRSS1 variants responsible for chronic pancreatitis: An expert perspective from the Franco-Chinese GREPAN study group.

Zheng Wang, Hong Zhang, C. Clavel, 2023, Pancreatology : official journal of the International Association of Pancreatology (IAP) ... [et al.].

Redox cofactors insertion in prokaryotic molybdoenzymes occurs via a conserved folding mechanism

A. Walburger, B. Guigliarelli, A. Magalon, 2016, Scientific Reports.

Membrane-bound respiratory nitrate reductase functioning: It takes two to tango

B. Guigliarelli, A. Magalon, P. Arnoux, 2012 .

Biogenesis of a Respiratory Complex Is Orchestrated by a Single Accessory Protein*

B. Guigliarelli, A. Magalon, S. Grimaldi, 2007, Journal of Biological Chemistry.

High-stability semiquinone intermediate in nitrate reductase A (NarGHI) from Escherichia coli is located in a quinol oxidation site close to heme bD.

B. Guigliarelli, A. Magalon, P. Bertrand, 2007, Biochemistry.