F. Biaso

发表

DFT investigation of the molybdenum cofactor in periplasmic nitrate reductases: structure of the Mo(V) EPR-active species.

B. Guigliarelli, B. Burlat, F. Biaso, 2012, Inorganic chemistry.

Single-domain flavoenzymes trigger lytic polysaccharide monooxygenases for oxidative degradation of cellulose

B. Henrissat, E. Record, H. Rogniaux, 2016, Scientific Reports.

Synthesis of a stable radical anion via the one electron reduction of a 1,1-bis-phosphinosulfide alkene derivative.

T. Cantat, M. Geoffroy, P. le Floch, 2008, Chemical communications.

Discovery of fungal oligosaccharide-oxidising flavo-enzymes with previously unknown substrates, redox-activity profiles and interplay with LPMOs

B. Henrissat, E. Master, B. Guigliarelli, 2020, Nature Communications.

Mutations in the coordination spheres of T1 Cu affect Cu2+-activation of the laccase from Thermus thermophilus.

Xie Wang, R. Clément, I. Mazurenko, 2021, Biochimie.

Tuning the redox properties of a [4Fe-4S] center to modulate the activity of Mo-bisPGD periplasmic nitrate reductase.

D. Pignol, G. Gerbaud, B. Guigliarelli, 2019, Biochimica et biophysica acta. Bioenergetics.

Reductive activation in periplasmic nitrate reductase involves chemical modifications of the Mo-cofactor beyond the first coordination sphere of the metal ion.

D. Pignol, B. Guigliarelli, P. Arnoux, 2014, Biochimica et biophysica acta.

The membrane-bound flavocytochrome MsrQ is a substrate of the cytosolic flavin reductase Fre in Escherichia coli

B. Guigliarelli, F. Fieschi, Corinne Vivès, 2022 .

Membrane-Bound Flavocytochrome MsrQ Is a Substrate of the Flavin Reductase Fre in Escherichia coli.

B. Guigliarelli, F. Fieschi, Corinne Vivès, 2021, ACS chemical biology.

Impact of copper ligand mutations on a cupredoxin with a green copper center.

G. Sciara, A. Vila, Xie Wang, 2017, Biochimica et biophysica acta. Bioenergetics.

High‐Field EPR Study of Frozen Aqueous Solutions of Iron(III) Citrate Complexes

F. Thomas, C. Duboc, B. Barbara, 2005 .

Electron transfer in an acidophilic bacterium: interaction between a diheme cytochrome and a cupredoxin

S. Lecomte, P. Mansuelle, L. Abriata, 2018, Chemical science.

Spectroscopic and Structural Characterization of Reduced Desulfovibrio vulgaris Hildenborough W-FdhAB Reveals Stable Metal Coordination during Catalysis

M. Romão, B. Guigliarelli, I. Pereira, 2022, ACS chemical biology.

Rigid Bis(tetrathiafulvalenes) Doubly Bridged by Phosphino Groups and Derivatives: Synthesis and Intramolecular Mixed Valence State

N. Avarvari, E. Levillain, M. Geoffroy, 2009 .

Copper Complexes as Bioinspired Models for Lytic Polysaccharide Monooxygenases.

M. Orio, B. Guigliarelli, Alda Lisa Concia, 2017, Inorganic chemistry.

Comparative studies on the iron chelators O-TRENSOX and TRENCAMS: selectivity of the complexation towards other biologically relevant metal ions and Al(3+).

G. Serratrice, J. Pierre, F. Biaso, 2002, Journal of inorganic biochemistry.

Intramolecular mixed-valence state through silicon or germanium double bridges in rigid bis(tetrathiafulvalenes).

N. Avarvari, E. Levillain, M. Geoffroy, 2007, Chemistry.

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

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

Helicate extension as a route to molecular wires.

K. Rissanen, C. Cramer, L. Gagliardi, 2008, Chemistry.

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.

Tetrathiafulvalene-phosphine-based iron and ruthenium carbonyl complexes: electrochemical and EPR studies.

N. Avarvari, E. Levillain, F. Sauvage, 2005, Physical chemistry chemical physics : PCCP.

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.

New trends in the chemistry of iron(III) citrate complexes: correlations between X-ray structures and solution species probed by electrospray mass spectrometry and kinetics of iron uptake from citrate by iron chelators.

I. Gautier-Luneau, C. Lebrun, G. Serratrice, 2005, Chemistry.

Formation and structure of a stable monoradical cation by reduction of a diphosphafulvenium salt.

T. Cantat, M. Geoffroy, P. le Floch, 2006, Angewandte Chemie.

Iron(III) Exchange Process between Hexadentate Tripodal Ligands: Models for the Ternary Complexes

A. Albrecht-Gary, S. Blanc, G. Serratrice, 2007 .

Mechanism of the Stepwise Dissociation of FeIII Complexes with Tripodal Ligands as Siderophore Models

F. Thomas, G. Serratrice, F. Biaso, 2004 .

Iron(III) chelation: Tuning of the pH dependence by mixed ligands

A. Albrecht-Gary, S. Blanc, F. Thomas, 2003 .

Detrimental effect of the 6 His C-terminal tag on YedY enzymatic activity and influence of the TAT signal sequence on YedY synthesis

D. Pignol, P. Arnoux, M. Sabaty, 2013, BMC Biochemistry.

Spectroscopic Characterization of a Green Copper Site in a Single-Domain Cupredoxin

G. Sciara, S. Caffarri, M. Roger, 2014, PloS one.

Electron transfer in an acidophilic bacterium: interaction between a diheme cytochrome and a cupredoxin † 4879 ChemicalScience EDGE

X. Wang, R. Clément, M. Roger, 2022 .

Electron transfer in an acidophilic bacterium: interaction between a diheme cytochrome and a cupredoxin † ChemicalScience EDGE ARTICLE

P. Mansuelle, X. Wang, R. Clément, 2018 .