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Catalytic roles for two water bridged residues (Asp-98 and His-255) in the active site of copper-containing nitrite reductaseStructure and site-directed mutagenesis of a flavoprotein from Escherichia coli that reduces nitrocompounds: alteration of pyridine nucleotide binding by a single amino acid substitutionCrystal structure of the soluble domain of the major anaerobically induced outer membrane protein (AniA) from pathogenic Neisseria: a new class of copper-containing nitrite reductasesX-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32Directing the mode of nitrite binding to a copper-containing nitrite reductase from Alcaligenes faecalis S-6: Characterization of an active site isoleucineReconstitution of the type-1 active site of the H145G/A variants of nitrite reductase by ligand insertionEffect of the methionine ligand on the reorganization energy of the type-1 copper site of nitrite reductaseHaem recognition by a Staphylococcus aureus NEAT domainStable copper-nitrosyl formation by nitrite reductase in either oxidation stateConserved active site residues limit inhibition of a copper-containing nitrite reductase by small moleculesRuffling of Metalloporphyrins Bound to IsdG and IsdI, Two Heme-degrading Enzymes in Staphylococcus aureusFerritin is used for iron storage in bloom-forming marine pennate diatomsCharacterization of staphyloferrin A biosynthetic and transport mutants in Staphylococcus aureusStructural and Mechanistic Studies of a Stabilized Subunit Dimer Variant of Escherichia coli Bacterioferritin Identify Residues Required for Core FormationDirected evolution of copper nitrite reductase to a chromogenic reductantThe IsdG-family of haem oxygenases degrades haem to a novel chromophoreStructure and function of P19, a high-affinity iron transporter of the human pathogen Campylobacter jejuniCharacterization of dye-decolorizing peroxidases from Rhodococcus jostii RHA1Unique Heme-Iron Coordination by the Hemoglobin Receptor IsdB of Staphylococcus aureusInactivation of the Heme Degrading Enzyme IsdI by an Active Site Substitution That Diminishes Heme RufflingImproved Manganese-Oxidizing Activity of DypB, a Peroxidase from a Lignolytic BacteriumMechanism of Ferrous Iron Binding and Oxidation by Ferritin from a Pennate DiatomSteric Mechanism of Auto-Inhibitory Regulation of Specific and Non-Specific DNA Binding by the ETS Transcriptional Repressor ETV6Structural and kinetic properties of Rhodobacter sphaeroides photosynthetic reaction centers containing exclusively Zn-coordinated bacteriochlorophyll as bacteriochlorin cofactorsSynthesis of L-2,3-diaminopropionic acid, a siderophore and antibiotic precursorDeciphering the Substrate Specificity of SbnA, the Enzyme Catalyzing the First Step in Staphyloferrin B BiosynthesisRaster3D Version 2.0. A program for photorealistic molecular graphicsA Diatom Ferritin Optimized for Iron Oxidation but Not Iron Storage.A Ferric-Peroxo Intermediate in the Oxidation of Heme by IsdI.Electronic properties of the highly ruffled heme bound to the heme degrading enzyme IsdI.Side-on copper-nitrosyl coordination by nitrite reductase.SbnG, a citrate synthase in Staphylococcus aureus: a new fold on an old enzyme.Helical shape of Helicobacter pylori requires an atypical glutamine as a zinc ligand in the carboxypeptidase Csd4The B-type channel is a major route for iron entry into the ferroxidase center and central cavity of bacterioferritin.Redox-coupled proton transfer mechanism in nitrite reductase revealed by femtosecond crystallography.The Mannoprotein Cig1 supports iron acquisition from heme and virulence in the pathogenic fungus Cryptococcus neoformans.A Bacterial Cell Shape-Determining Inhibitor.Type-2 copper-containing enzymes.Iron core mineralisation in prokaryotic ferritins.Iron Uptake Oxidoreductase (IruO) Uses a Flavin Adenine Dinucleotide Semiquinone Intermediate for Iron-Siderophore Reduction.
P50
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P50
description
researcher
@en
wetenschapper
@nl
name
M E Murphy
@en
M E Murphy
@nl
type
label
M E Murphy
@en
M E Murphy
@nl
prefLabel
M E Murphy
@en
M E Murphy
@nl
P106
P31
P496
0000-0003-2589-0014