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Structure and Cu(I)-binding properties of the N-terminal soluble domains of Bacillus subtilis CopAEffects of substitutions in the CXXC active-site motif of the extracytoplasmic thioredoxin ResAStructure and Functional Properties of Bacillus subtilis Endospore Biogenesis Factor StoAStructural basis for iron mineralization by bacterioferritinStructural and Mechanistic Studies of a Stabilized Subunit Dimer Variant of Escherichia coli Bacterioferritin Identify Residues Required for Core FormationCrystal Structure and Biophysical Properties of Bacillus subtilis BdbD: AN OXIDIZING THIOL:DISULFIDE OXIDOREDUCTASE CONTAINING A NOVEL METAL SITEMonitoring the iron status of the ferroxidase center of Escherichia coli bacterioferritin using fluorescence spectroscopyA tetranuclear Cu(I) cluster in the metallochaperone protein CopZMechanism of Ferrous Iron Binding and Oxidation by Ferritin from a Pennate DiatomFerritins: furnishing proteins with ironCu(I)- and proton-binding properties of the first N-terminal soluble domain of Bacillus subtilis CopAA Diatom Ferritin Optimized for Iron Oxidation but Not Iron Storage.Characterization of [4Fe-4S]-containing and cluster-free forms of Streptomyces WhiD.Nitrosylation of Nitric-Oxide-Sensing Regulatory Proteins Containing [4Fe-4S] Clusters Gives Rise to Multiple Iron-Nitrosyl Complexes.The transcriptional repressor protein NsrR senses nitric oxide directly via a [2Fe-2S] cluster.Cmr is a redox-responsive regulator of DosR that contributes to M. tuberculosis virulence.The dddP gene of Roseovarius nubinhibens encodes a novel lyase that cleaves dimethylsulfoniopropionate into acrylate plus dimethyl sulfide.Mechanistic insight into the nitrosylation of the [4Fe-4S] cluster of WhiB-like proteinsThe B-type channel is a major route for iron entry into the ferroxidase center and central cavity of bacterioferritin.NsrR from Streptomyces coelicolor is a nitric oxide-sensing [4Fe-4S] cluster protein with a specialized regulatory function.Superoxide-mediated amplification of the oxygen-induced switch from [4Fe-4S] to [2Fe-2S] clusters in the transcriptional regulator FNR.The role of ResA in type II cytochrome c maturation.Reversible cycling between cysteine persulfide-ligated [2Fe-2S] and cysteine-ligated [4Fe-4S] clusters in the FNR regulatory protein.Atx1-like chaperones and their cognate P-type ATPases: copper-binding and transfer.The O2 sensitivity of the transcription factor FNR is controlled by Ser24 modulating the kinetics of [4Fe-4S] to [2Fe-2S] conversion.Reactions of nitric oxide and oxygen with the regulator of fumarate and nitrate reduction, a global transcriptional regulator, during anaerobic growth of Escherichia coli.NBP35 interacts with DRE2 in the maturation of cytosolic iron-sulphur proteins in Arabidopsis thaliana.There's NO stopping NsrR, a global regulator of the bacterial NO stress response.Iron core mineralisation in prokaryotic ferritins.Bacterial iron-sulfur regulatory proteins as biological sensor-switchesMechanisms of iron mineralization in ferritins: one size does not fit all.Iron-sulfur clusters as biological sensors: the chemistry of reactions with molecular oxygen and nitric oxide.Site-directed replacement of the coaxial heme ligands of bacterioferritin generates heme-free variants.Biochemical properties of Paracoccus denitrificans FnrP: reactions with molecular oxygen and nitric oxide.Mass spectrometric identification of intermediates in the O2-driven [4Fe-4S] to [2Fe-2S] cluster conversion in FNR.Kinetic analysis of copper transfer from a chaperone to its target protein mediated by complex formation.Diversity of Fe2+ entry and oxidation in ferritins.Mass spectrometry of B. subtilis CopZ: Cu(i)-binding and interactions with bacillithiol.Mechanism of [4Fe-4S](Cys)4 cluster nitrosylation is conserved among NO-responsive regulators.Heme binding to the second, lower-affinity site of the global iron regulator Irr from Rhizobium leguminosarum promotes oligomerization.
P50
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P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Nick E Le Brun
@ast
Nick E Le Brun
@en
Nick E Le Brun
@es
Nick E Le Brun
@nl
Nick E Le Brun
@sl
type
label
Nick E Le Brun
@ast
Nick E Le Brun
@en
Nick E Le Brun
@es
Nick E Le Brun
@nl
Nick E Le Brun
@sl
prefLabel
Nick E Le Brun
@ast
Nick E Le Brun
@en
Nick E Le Brun
@es
Nick E Le Brun
@nl
Nick E Le Brun
@sl
P106
P1153
6603863121
P21
P31
P496
0000-0001-9780-4061