about
Measurement of the heme affinity for yeast dap1p, and its importance in cellular functionBiophysical and structural analysis of a novel heme B iron ligation in the flavocytochrome cellobiose dehydrogenaseBiochemical and structural characterization of Pseudomonas aeruginosa Bfd and FPR: ferredoxin NADP+ reductase and not ferredoxin is the redox partner of heme oxygenase under iron-starvation conditionsStructural Characterization of the Hemophore HasAp from Pseudomonas aeruginosa : NMR Spectroscopy Reveals Protein−Protein Interactions between Holo-HasAp and Hemoglobin † , ‡The Hemophore HasA from Yersinia pestis (HasA yp ) Coordinates Hemin with a Single Residue, Tyr75, and with Minimal Conformational ChangeReplacing the Axial Ligand Tyrosine 75 or Its Hydrogen Bond Partner Histidine 83 Minimally Affects Hemin Acquisition by the Hemophore HasAp from Pseudomonas aeruginosaFungal heme oxygenases: Functional expression and characterization of Hmx1 from Saccharomyces cerevisiae and CaHmx1 from Candida albicans.DevS, a heme-containing two-component oxygen sensor of Mycobacterium tuberculosisCharacterizing millisecond intermediates in hemoproteins using rapid-freeze-quench resonance Raman spectroscopy.Calculated and experimental spin state of seleno cytochrome P450.Transcription Factor NsrR from Bacillus subtilis Senses Nitric Oxide with a 4Fe-4S Cluster (†)Kinetic and spectroscopic studies of hemin acquisition in the hemophore HasAp from Pseudomonas aeruginosa.Light-induced N₂O production from a non-heme iron-nitrosyl dimer.Spectroscopic characterization of heme iron-nitrosyl species and their role in NO reductase mechanisms in diiron proteins.Nitric oxide dioxygenation reaction in DevS and the initial response to nitric oxide in Mycobacterium tuberculosisThioether-ligated iron(II) and iron(III)-hydroperoxo/alkylperoxo complexes with an H-bond donor in the second coordination sphere.Spectroscopic characterization of mononitrosyl complexes in heme--nonheme diiron centers within the myoglobin scaffold (Fe(B)Mbs): relevance to denitrifying NO reductaseProximal ligand electron donation and reactivity of the cytochrome P450 ferric-peroxo anionVibrational analysis of mononitrosyl complexes in hemerythrin and flavodiiron proteins: relevance to detoxifying NO reductase.Ion-binding properties of a K+ channel selectivity filter in different conformations.Fourier transform infrared characterization of a CuB-nitrosyl complex in cytochrome ba3 from Thermus thermophilus: relevance to NO reductase activity in heme-copper terminal oxidases.Accommodation of two diatomic molecules in cytochrome bo: insights into NO reductase activity in terminal oxidasesA distal tyrosine residue is required for ligand discrimination in DevS from Mycobacterium tuberculosis.The production of nitrous oxide by the heme/nonheme diiron center of engineered myoglobins (Fe(B)Mbs) proceeds through a trans-iron-nitrosyl dimer.Effect of Outer-Sphere Side Chain Substitutions on the Fate of the trans Iron-Nitrosyl Dimer in Heme/Nonheme Engineered Myoglobins (Fe(B)Mbs): Insights into the Mechanism of Denitrifying NO ReductasesReactivity studies on Fe(III)-(O2(2-))-Cu(II) compounds: influence of the ligand architecture and copper ligand denticity.Dioxygen reactivity of copper and heme-copper complexes possessing an imidazole-phenol cross-link.Photoinitiated Reactivity of a Thiolate-Ligated, Spin-Crossover Nonheme {FeNO}(7) Complex with Dioxygen.Structure of the primary electron donor in photosystem I: a resonance Raman study.Secondary coordination sphere influence on the reactivity of nonheme iron(II) complexes: an experimental and DFT approach.Distal Hydrogen-bonding Interactions in Ligand Sensing and Signaling by Mycobacterium tuberculosis DosS.Rational reprogramming of the R2 subunit of Escherichia coli ribonucleotide reductase into a self-hydroxylating monooxygenase.Oxidation of heme to beta- and delta-biliverdin by Pseudomonas aeruginosa heme oxygenase as a consequence of an unusual seating of the heme.Coupled oxidation vs heme oxygenation: insights from axial ligand mutants of mitochondrial cytochrome b5.Cloning and expression of a heme binding protein from the genome of Saccharomyces cerevisiae.Characterization of NO adducts of the diiron center in protein R2 of Escherichia coli ribonucleotide reductase and site-directed variants; implications for the O2 activation mechanism.Heme-copper/dioxygen adduct formation relevant to cytochrome c oxidase: spectroscopic characterization of [(6L)FeIII-(O2(2-))-CuII]+.Reduction of the ferrous alpha-verdoheme-cytochrome b5 complex.Heme/non-heme diiron(II) complexes and O2, CO, and NO adducts as reduced and substrate-bound models for the active site of bacterial nitric oxide reductase.A Six-Coordinate Peroxynitrite Low-Spin Iron(III) Porphyrinate Complex-The Product of the Reaction of Nitrogen Monoxide (·NO(g)) with a Ferric-Superoxide Species.
P50
Q24658256-754C71DC-0345-4CA0-9E66-09C720CB1B4AQ27641420-A75C29DB-D144-4A1C-9C6A-1C8B0F0AC109Q27648714-C121D7AB-BABE-411C-B7D1-89F5F4A069F4Q27653104-5EA3711C-6251-4AD6-A726-AB63CA7A223FQ27677321-1CEF44B4-B956-4D73-9C3C-C451A48BDBE4Q27682167-20F3DE57-BF8E-4B42-B6A0-3E6B22F1FFD5Q27930565-A58A3761-174B-497C-9D76-164D474CA4A9Q28486549-9BB0BEF7-755E-4675-9002-16CF3422E3C7Q33637944-039D4E0C-490C-4187-B1FF-5B9358455205Q33766095-FC625A6E-E6D5-4E38-A76A-8E8FA2BDA6C5Q33936719-B26A4428-FE08-4AB1-9636-3840B295FD49Q34039869-47CF72C5-99A3-4044-B191-118A7BFD6539Q34160488-C4A285AD-C3C8-4D3E-BE89-5F9DFB580738Q34528275-FF3655DF-4E9D-449E-81B2-AD290F87E375Q34815766-56EE9171-D823-4BEA-AF64-E080A46CA364Q35057995-B5D9CB40-A9F7-46AF-8389-F574502FF863Q35074627-E4D34C81-ED7A-4FBB-ADFD-4D84457A0D4FQ35897516-0D19946E-C4FD-4F9D-A309-A6B33177F8EDQ35911051-7717E00F-2056-477C-B1D1-140D13545E66Q36371331-56629930-1046-4332-B787-533FA7A2B492Q36901765-6DCCADBF-F0C1-4636-B2B7-D4C6E7B6CEC1Q37116990-50CFF0C9-11ED-4CB0-AFFB-451242945FA1Q37151533-C85A52C2-20DD-4EFD-B257-32BBB0CE027AQ37731552-8ABA71C0-A400-4821-93D8-71C515E14269Q39775133-B7B79FF1-4C10-4807-A11E-C04ED15A7FC1Q40196859-F2CB3C5F-45DB-483D-86EB-641A31E08903Q40442665-1437352B-2BBF-451C-A2EC-85D027D92F22Q40965272-66B4C42C-0F64-4B17-BEE4-2CE228B432FDQ41235185-1AC79581-8F23-4218-BADD-E1A44BC3DEC8Q41978216-BA2CEF51-3BC0-4A34-9341-489A16AD7A2DQ42395491-D8CBCE03-4E2E-4BB1-90C0-698F3F14404AQ43679732-FFEFA667-5CFA-4C12-8237-1CA5C2F3C01AQ44244382-155C47B3-7AE6-47CA-A8B6-EA97860D1D96Q44386744-05119D10-5AD6-4ABE-BE24-688A7DF70DA3Q44406359-9C1A89EA-B11D-4E79-B65E-4D7E983CA104Q45018456-3ED2CF3B-C8C5-41C2-ADC2-BBD366F4964DQ45177166-80C6A247-2178-4BA7-8417-140D4FCF62D4Q45191835-2630D8F5-59B8-4F33-AFC4-B130C7C01F41Q45310097-A9220239-4BDA-4F5B-A5EB-0E53CD439BCAQ46014439-CB01B47C-09C8-4A60-BC1A-FD25017EAB65
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Pierre Moenne-Loccoz
@ast
Pierre Moenne-Loccoz
@en
Pierre Moenne-Loccoz
@es
Pierre Moenne-Loccoz
@nl
type
label
Pierre Moenne-Loccoz
@ast
Pierre Moenne-Loccoz
@en
Pierre Moenne-Loccoz
@es
Pierre Moenne-Loccoz
@nl
prefLabel
Pierre Moenne-Loccoz
@ast
Pierre Moenne-Loccoz
@en
Pierre Moenne-Loccoz
@es
Pierre Moenne-Loccoz
@nl
P106
P1153
7004746746
P31
P496
0000-0002-7684-7617