@prefix dcat: <http://www.w3.org/ns/dcat#> .
@prefix dct: <http://purl.org/dc/terms/> .
@prefix foaf: <http://xmlns.com/foaf/0.1/> .
@prefix vcard: <http://www.w3.org/2006/vcard/ns#> .
@prefix xsd: <http://www.w3.org/2001/XMLSchema#> .

<https://rec.harvest-normandie.data4citizen.com/dataset/oai-hal-pasteur-00974717v1> a dcat:Dataset ;
    dct:description """
              In nitrite reductase (cd(1) NIR), the c-heme mediates electron transfer to the catalytic d(1)-heme where nitrite (NO(2)(-)) is reduced to nitric oxide (NO). An interesting feature of this enzyme is the relative lability of the reaction product NO bound to the d(1)-heme. Marked differences in the c- to d(1)-heme electron-transfer rates were reported for cd(1) NIRs from different sources, such as Pseudomonas stutzeri (P. stutzeri) and Pseudomonas aeruginosa (P. aeruginosa). The three-dimensional structure of the P. aeruginosa enzyme has been determined, but that of the P. stutzeri enzyme is still unknown. The difference in electron transfer rates prompted a comparison of the structural properties of the d(1)-heme pocket of P. stutzeri cd(1) NIR with those of the P. aeruginosa wild type enzyme (WT) and its Y10F using their nitrosyl d(1)-heme complexes. We applied high field pulse electron paramagnetic resonance (EPR) techniques that detect nuclear spins in the close environment of the spin bearing Fe(II)-NO entity. We observed similarities in the rhombic g-tensor and detected a proximal histidine ligand with (14)N hyperfine and quadrupole interactions also similar to those of P. aeruginosa WT and Y10F mutant complexes. In contrast, we also observed significant differences in the H-bond network involving the NO ligand and a larger solvent accessibility for P. stutzeri attributed to the absence of this tyrosine residue. For P. aeruginosa, cd(1) NIR domain swapping allows Tyr(10) to become H-bonded to the bound NO substrate. These findings support a previous suggestion that the large difference in the c- to d(1)-heme electron transfer rates between the two enzymes is related to solvent accessibility of their d(1)-heme pockets.
            """ ;
    dct:identifier "pasteur-00974717" ;
    dct:issued "2026-05-05T16:16:40.376097"^^xsd:dateTime ;
    dct:language "en" ;
    dct:modified "2026-05-05T16:16:40.376102"^^xsd:dateTime ;
    dct:publisher <https://rec.harvest-normandie.data4citizen.com/organization/cce9db95-46d9-4dc2-84b6-764215d0a002> ;
    dct:title "Solvent accessibility in the distal heme pocket of the nitrosyl d(1)-heme complex of Pseudomonas stutzeri cd(1) nitrite reductase." ;
    dcat:contactPoint [ a vcard:Organization ;
            vcard:fn "CCSD" ] ;
    dcat:distribution <https://rec.harvest-normandie.data4citizen.com/dataset/oai-hal-pasteur-00974717v1/resource/12e3029e-a12b-4517-9e35-25416175e378> ;
    dcat:keyword "infoeu-reposemanticsarticle",
        "journal-articles",
        "mesh-cytochromes",
        "mesh-deuterium-exchange-measurement",
        "mesh-electron-spin-resonance-spectroscopy",
        "mesh-heme",
        "mesh-nitrite-reductases",
        "mesh-pseudomonas-aeruginosa",
        "mesh-pseudomonas-stutzeri",
        "mesh-spectrophotometry-ultraviolet",
        "sdvbbmlife-sciences-q-biobiochemistry-molecular-biology" ;
    dcat:landingPage <ISSN:%200006-2960> .

<ISSN:%200006-2960> a foaf:Document .

<https://rec.harvest-normandie.data4citizen.com/dataset/oai-hal-pasteur-00974717v1/resource/12e3029e-a12b-4517-9e35-25416175e378> a dcat:Distribution ;
    dct:format "HTML" ;
    dct:issued "2026-05-05T16:16:40.383458"^^xsd:dateTime ;
    dct:modified "2026-05-05T16:16:40.365211"^^xsd:dateTime ;
    dct:title "Solvent accessibility in the distal heme pocket of the nitrosyl d(1)-heme complex of Pseudomonas stutzeri cd(1) nitrite reductase." ;
    dcat:accessURL <https://riip.hal.science/pasteur-00974717> .

<https://rec.harvest-normandie.data4citizen.com/organization/cce9db95-46d9-4dc2-84b6-764215d0a002> a foaf:Agent ;
    foaf:name "test_moissonnage_selune" .