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The crystal structure of HasA, a hemophore secreted by Serratia marcescensStructural and redox plasticity in the heterodimeric periplasmic nitrate reductaseA Structural Basis for the pH-Dependent Xanthophyll Cycle in Arabidopsis thalianaThe crystallographic structure of thermoNicotianamine synthase with a synthetic reaction intermediate highlights the sequential processing mechanismStructural insight into magnetochrome-mediated magnetite biomineralizationSulphur shuttling across a chaperone during molybdenum cofactor maturationA papain-like enzyme at work: native and acyl-enzyme intermediate structures in phytochelatin synthesis.Detrimental effect of the 6 His C-terminal tag on YedY enzymatic activity and influence of the TAT signal sequence on YedY synthesis.Cardiolipin-based respiratory complex activation in bacteria.Structure and evolution of the magnetochrome domains: no longer alone.Cardiolipin binding in bacterial respiratory complexes: structural and functional implications.Biosynthesis of a broad-spectrum nicotianamine-like metallophore in Staphylococcus aureus.Dependence of catalytic activity on driving force in solution assays and protein film voltammetry: insights from the comparison of nitrate reductase mutants.Characterization of a novel Drosophila melanogaster galectin. Expression in developing immune, neural, and muscle tissues.Reductive activation in periplasmic nitrate reductase involves chemical modifications of the Mo-cofactor beyond the first coordination sphere of the metal ion.Cu binding by the Escherichia coli metal-efflux accessory protein RcnB.In Rhodobacter sphaeroides respiratory nitrate reductase, the kinetics of substrate binding favors intramolecular electron transfer.Structural and thermodynamic studies on cation-Pi interactions in lectin-ligand complexes: high-affinity galectin-3 inhibitors through fine-tuning of an arginine-arene interaction.Comparative genomic analysis provides insights into the evolution and niche adaptation of marine Magnetospira sp. QH-2 strain.Major Mo(V) EPR signature of Rhodobacter sphaeroides periplasmic nitrate reductase arising from a dead-end species that activates upon reduction. Relation to other molybdoenzymes from the DMSO reductase family.Pseudomonas aeruginosa zinc uptake in chelating environment is primarily mediated by the metallophore pseudopaline.An algal photoenzyme converts fatty acids to hydrocarbons.Independent and cooperative regulation of staphylopine biosynthesis and trafficking by Fur and Zur.Effects of slow substrate binding and release in redox enzymes: theory and application to periplasmic nitrate reductase.methionine sulfoxide reductase P reduces ‑ and ‑diastereomers of methionine sulfoxide from a broad‑spectrum of protein substratesPhoto-induced electron transfer in intact cells of Rubrivivax gelatinosus mutants deleted in the RC-bound tetraheme cytochrome: Insight into evolution of photosynthetic electron transportKinetics of substrate inhibition of periplasmic nitrate reductaseReassessing the Strategies for Trapping Catalytic Intermediates during Nitrate Reductase TurnoverCorrecting for Electrocatalyst Desorption and Inactivation in Chronoamperometry ExperimentsAccess to the Active Site of Periplasmic Nitrate Reductase: Insights from Site-Directed Mutagenesis and Zinc Inhibition Studies†Crystal structure of the transcriptional repressor DdrO: insight into the metalloprotease/repressor-controlled radiation response in DeinococcusTuning the redox properties of a [4Fe-4S] center to modulate the activity of Mo-bisPGD periplasmic nitrate reductaseSimple rules govern the diversity of bacterial nicotianamine-like metallophoresControl by Metals of Staphylopine Dehydrogenase Activity during Metallophore Biosynthesis
P50
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P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Pascal Arnoux
@ast
Pascal Arnoux
@en
Pascal Arnoux
@es
Pascal Arnoux
@nl
type
label
Pascal Arnoux
@ast
Pascal Arnoux
@en
Pascal Arnoux
@es
Pascal Arnoux
@nl
prefLabel
Pascal Arnoux
@ast
Pascal Arnoux
@en
Pascal Arnoux
@es
Pascal Arnoux
@nl
P106
P21
P31
P496
0000-0003-4609-4893