Hydrogen bonding to the cysteine ligand of superoxide reductase: acid–base control of the reaction intermediates View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2013-08-06

AUTHORS

Emilie Tremey, Florence Bonnot, Yohann Moreau, Catherine Berthomieu, Alain Desbois, Vincent Favaudon, Geneviève Blondin, Chantal Houée-Levin, Vincent Nivière

ABSTRACT

Superoxide reductase (SOR) is a non-heme iron metalloenzyme that detoxifies superoxide radical in microorganisms. Its active site consists of an unusual non-heme Fe2+ center in a [His4Cys1] square pyramidal pentacoordination, with the axial cysteine ligand proposed to be an essential feature in catalysis. Two NH peptide groups from isoleucine 118 and histidine 119 establish hydrogen bonds involving the sulfur ligand (Desulfoarculus baarsii SOR numbering). To investigate the catalytic role of these hydrogen bonds, the isoleucine 118 residue of the SOR from Desulfoarculus baarsii was mutated into alanine, aspartate, or serine residues. Resonance Raman spectroscopy showed that the mutations specifically induced an increase of the strength of the Fe3+–S(Cys) and S–Cβ(Cys) bonds as well as a change in conformation of the cysteinyl side chain, which was associated with the alteration of the NH hydrogen bonding involving the sulfur ligand. The effects of the isoleucine mutations on the reactivity of SOR with O2•− were investigated by pulse radiolysis. These studies showed that the mutations induced a specific increase of the pKa of the first reaction intermediate, recently proposed to be an Fe2+–O2•− species. These data were supported by density functional theory calculations conducted on three models of the Fe2+–O2•− intermediate, with one, two, or no hydrogen bonds involving the sulfur ligand. Our results demonstrated that the hydrogen bonds between the NH (peptide) and the cysteine ligand tightly control the rate of protonation of the Fe2+–O2•− reaction intermediate to form an Fe3+–OOH species. More... »

PAGES

815-830

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00775-013-1025-1

DOI

http://dx.doi.org/10.1007/s00775-013-1025-1

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1038119476

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/23917995


Indexing Status Check whether this publication has been indexed by Scopus and Web Of Science using the SN Indexing Status Tool
Incoming Citations Browse incoming citations for this publication using opencitations.net

JSON-LD is the canonical representation for SciGraph data.

TIP: You can open this SciGraph record using an external JSON-LD service: JSON-LD Playground Google SDTT

[
  {
    "@context": "https://springernature.github.io/scigraph/jsonld/sgcontext.json", 
    "about": [
      {
        "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/03", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Chemical Sciences", 
        "type": "DefinedTerm"
      }, 
      {
        "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/0306", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Physical Chemistry (incl. Structural)", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Catalytic Domain", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Cysteine", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Hydrogen Bonding", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Hydrogen-Ion Concentration", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Ligands", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Models, Molecular", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Mutagenesis, Site-Directed", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Mutation", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Oxidation-Reduction", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Oxidoreductases", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Proteobacteria", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Quantum Theory", 
        "type": "DefinedTerm"
      }
    ], 
    "author": [
      {
        "affiliation": {
          "alternateName": "Universit\u00e9 de Grenoble, 38000, Grenoble, France", 
          "id": "http://www.grid.ac/institutes/grid.9621.c", 
          "name": [
            "Laboratoire de Chimie et Biologie des M\u00e9taux, CEA, iRTSV, 17 avenue des Martyrs, 38054, Grenoble, France", 
            "CNRS, UMR 5249, 38054, Grenoble, France", 
            "Universit\u00e9 de Grenoble, 38000, Grenoble, France"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Tremey", 
        "givenName": "Emilie", 
        "id": "sg:person.01307624625.23", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01307624625.23"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Universit\u00e9 de Grenoble, 38000, Grenoble, France", 
          "id": "http://www.grid.ac/institutes/grid.9621.c", 
          "name": [
            "Laboratoire de Chimie et Biologie des M\u00e9taux, CEA, iRTSV, 17 avenue des Martyrs, 38054, Grenoble, France", 
            "CNRS, UMR 5249, 38054, Grenoble, France", 
            "Universit\u00e9 de Grenoble, 38000, Grenoble, France"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Bonnot", 
        "givenName": "Florence", 
        "id": "sg:person.0636707711.52", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0636707711.52"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Universit\u00e9 de Grenoble, 38000, Grenoble, France", 
          "id": "http://www.grid.ac/institutes/grid.9621.c", 
          "name": [
            "Laboratoire de Chimie et Biologie des M\u00e9taux, CEA, iRTSV, 17 avenue des Martyrs, 38054, Grenoble, France", 
            "CNRS, UMR 5249, 38054, Grenoble, France", 
            "Universit\u00e9 de Grenoble, 38000, Grenoble, France"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Moreau", 
        "givenName": "Yohann", 
        "id": "sg:person.01021251511.66", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01021251511.66"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Laboratoire Des Interactions Prot\u00e9ine M\u00e9tal, SBVME-CEA Cadarache/CNRS/Universit\u00e9 Aix-Marseille II, 13108, Saint-Paul-lez-Durance Cedex, France", 
          "id": "http://www.grid.ac/institutes/grid.5399.6", 
          "name": [
            "Laboratoire Des Interactions Prot\u00e9ine M\u00e9tal, SBVME-CEA Cadarache/CNRS/Universit\u00e9 Aix-Marseille II, 13108, Saint-Paul-lez-Durance Cedex, France"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Berthomieu", 
        "givenName": "Catherine", 
        "id": "sg:person.0641716334.91", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0641716334.91"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Laboratoire Stress Oxydant et D\u00e9toxication, SB2SM and CNRS UMR 8221, iBiTec-S, CEA Saclay, 91191, Gif-sur-Yvette Cedex, France", 
          "id": "http://www.grid.ac/institutes/grid.457334.2", 
          "name": [
            "Laboratoire Stress Oxydant et D\u00e9toxication, SB2SM and CNRS UMR 8221, iBiTec-S, CEA Saclay, 91191, Gif-sur-Yvette Cedex, France"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Desbois", 
        "givenName": "Alain", 
        "id": "sg:person.01216650776.59", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01216650776.59"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Inserm Unit\u00e9 612 and Institut Curie, B\u00e2timent 110-112, Centre Universitaire, 91405, Orsay Cedex, France", 
          "id": "http://www.grid.ac/institutes/grid.5842.b", 
          "name": [
            "Inserm Unit\u00e9 612 and Institut Curie, B\u00e2timent 110-112, Centre Universitaire, 91405, Orsay Cedex, France"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Favaudon", 
        "givenName": "Vincent", 
        "id": "sg:person.071237417.08", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.071237417.08"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Universit\u00e9 de Grenoble, 38000, Grenoble, France", 
          "id": "http://www.grid.ac/institutes/grid.9621.c", 
          "name": [
            "Laboratoire de Chimie et Biologie des M\u00e9taux, CEA, iRTSV, 17 avenue des Martyrs, 38054, Grenoble, France", 
            "CNRS, UMR 5249, 38054, Grenoble, France", 
            "Universit\u00e9 de Grenoble, 38000, Grenoble, France"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Blondin", 
        "givenName": "Genevi\u00e8ve", 
        "id": "sg:person.0657101562.93", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0657101562.93"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Laboratoire de Chimie Physique, CNRS/Universit\u00e9 Paris-Sud, B\u00e2timent 350, Centre Universitaire, 91405, Orsay Cedex, France", 
          "id": "http://www.grid.ac/institutes/grid.462861.f", 
          "name": [
            "Laboratoire de Chimie Physique, CNRS/Universit\u00e9 Paris-Sud, B\u00e2timent 350, Centre Universitaire, 91405, Orsay Cedex, France"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Hou\u00e9e-Levin", 
        "givenName": "Chantal", 
        "id": "sg:person.01203613311.33", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01203613311.33"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Universit\u00e9 de Grenoble, 38000, Grenoble, France", 
          "id": "http://www.grid.ac/institutes/grid.9621.c", 
          "name": [
            "Laboratoire de Chimie et Biologie des M\u00e9taux, CEA, iRTSV, 17 avenue des Martyrs, 38054, Grenoble, France", 
            "CNRS, UMR 5249, 38054, Grenoble, France", 
            "Universit\u00e9 de Grenoble, 38000, Grenoble, France"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Nivi\u00e8re", 
        "givenName": "Vincent", 
        "id": "sg:person.01044625215.48", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01044625215.48"
        ], 
        "type": "Person"
      }
    ], 
    "citation": [
      {
        "id": "sg:pub.10.1038/nchembio.85", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1021452802", 
          "https://doi.org/10.1038/nchembio.85"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1007/s00775-006-0104-y", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1010325438", 
          "https://doi.org/10.1007/s00775-006-0104-y"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1007/s007750050064", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1041779936", 
          "https://doi.org/10.1007/s007750050064"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1007/s00775-003-0465-4", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1023330125", 
          "https://doi.org/10.1007/s00775-003-0465-4"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1007/s007750050184", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1027260643", 
          "https://doi.org/10.1007/s007750050184"
        ], 
        "type": "CreativeWork"
      }
    ], 
    "datePublished": "2013-08-06", 
    "datePublishedReg": "2013-08-06", 
    "description": "Superoxide reductase (SOR) is a non-heme iron metalloenzyme that detoxifies superoxide radical in microorganisms. Its active site consists of an unusual non-heme Fe2+ center in a [His4Cys1] square pyramidal pentacoordination, with the axial cysteine ligand proposed to be an essential feature in catalysis. Two NH peptide groups from isoleucine 118 and histidine 119 establish hydrogen bonds involving the sulfur ligand (Desulfoarculus baarsii SOR numbering). To investigate the catalytic role of these hydrogen bonds, the isoleucine 118 residue of the SOR from Desulfoarculus baarsii was mutated into alanine, aspartate, or serine residues. Resonance Raman spectroscopy showed that the mutations specifically induced an increase of the strength of the Fe3+\u2013S(Cys) and S\u2013C\u03b2(Cys) bonds as well as a change in conformation of the cysteinyl side chain, which was associated with the alteration of the NH hydrogen bonding involving the sulfur ligand. The effects of the isoleucine mutations on the reactivity of SOR with O2\u2022\u2212 were investigated by pulse radiolysis. These studies showed that the mutations induced a specific increase of the pKa of the first reaction intermediate, recently proposed to be an Fe2+\u2013O2\u2022\u2212 species. These data were supported by density functional theory calculations conducted on three models of the Fe2+\u2013O2\u2022\u2212 intermediate, with one, two, or no hydrogen bonds involving the sulfur ligand. Our results demonstrated that the hydrogen bonds between the NH (peptide) and the cysteine ligand tightly control the rate of protonation of the Fe2+\u2013O2\u2022\u2212 reaction intermediate to form an Fe3+\u2013OOH species.", 
    "genre": "article", 
    "id": "sg:pub.10.1007/s00775-013-1025-1", 
    "isAccessibleForFree": true, 
    "isPartOf": [
      {
        "id": "sg:journal.1116242", 
        "issn": [
          "0949-8257", 
          "1432-1327"
        ], 
        "name": "JBIC Journal of Biological Inorganic Chemistry", 
        "publisher": "Springer Nature", 
        "type": "Periodical"
      }, 
      {
        "issueNumber": "7", 
        "type": "PublicationIssue"
      }, 
      {
        "type": "PublicationVolume", 
        "volumeNumber": "18"
      }
    ], 
    "keywords": [
      "sulfur ligands", 
      "hydrogen bonds", 
      "cysteine ligands", 
      "hydrogen bonding", 
      "NH hydrogen bonding", 
      "density functional theory calculations", 
      "first reaction intermediate", 
      "resonance Raman spectroscopy", 
      "non-heme Fe2", 
      "functional theory calculations", 
      "rate of protonation", 
      "axial cysteine ligand", 
      "OOH species", 
      "iron metalloenzyme", 
      "reaction intermediates", 
      "cysteinyl side chains", 
      "superoxide reductase", 
      "Raman spectroscopy", 
      "pulse radiolysis", 
      "theory calculations", 
      "active site", 
      "side chains", 
      "Desulfoarculus baarsii", 
      "peptide groups", 
      "catalytic role", 
      "ligands", 
      "bonds", 
      "acid-base control", 
      "Fe2", 
      "bonding", 
      "intermediates", 
      "reaction", 
      "pentacoordination", 
      "catalysis", 
      "protonation", 
      "spectroscopy", 
      "metalloenzymes", 
      "radiolysis", 
      "conformation", 
      "reactivity", 
      "residues", 
      "NH", 
      "reductase", 
      "chain", 
      "calculations", 
      "species", 
      "isoleucine mutation", 
      "serine residues", 
      "alanine", 
      "SOR", 
      "sites", 
      "microorganisms", 
      "essential features", 
      "strength", 
      "detoxifies", 
      "increase", 
      "group", 
      "aspartate", 
      "effect", 
      "center", 
      "rate", 
      "results", 
      "study", 
      "changes", 
      "features", 
      "role", 
      "data", 
      "model", 
      "alterations", 
      "control", 
      "mutations", 
      "specific increase"
    ], 
    "name": "Hydrogen bonding to the cysteine ligand of superoxide reductase: acid\u2013base control of the reaction intermediates", 
    "pagination": "815-830", 
    "productId": [
      {
        "name": "dimensions_id", 
        "type": "PropertyValue", 
        "value": [
          "pub.1038119476"
        ]
      }, 
      {
        "name": "doi", 
        "type": "PropertyValue", 
        "value": [
          "10.1007/s00775-013-1025-1"
        ]
      }, 
      {
        "name": "pubmed_id", 
        "type": "PropertyValue", 
        "value": [
          "23917995"
        ]
      }
    ], 
    "sameAs": [
      "https://doi.org/10.1007/s00775-013-1025-1", 
      "https://app.dimensions.ai/details/publication/pub.1038119476"
    ], 
    "sdDataset": "articles", 
    "sdDatePublished": "2022-10-01T06:38", 
    "sdLicense": "https://scigraph.springernature.com/explorer/license/", 
    "sdPublisher": {
      "name": "Springer Nature - SN SciGraph project", 
      "type": "Organization"
    }, 
    "sdSource": "s3://com-springernature-scigraph/baseset/20221001/entities/gbq_results/article/article_603.jsonl", 
    "type": "ScholarlyArticle", 
    "url": "https://doi.org/10.1007/s00775-013-1025-1"
  }
]
 

Download the RDF metadata as:  json-ld nt turtle xml License info

HOW TO GET THIS DATA PROGRAMMATICALLY:

JSON-LD is a popular format for linked data which is fully compatible with JSON.

curl -H 'Accept: application/ld+json' 'https://scigraph.springernature.com/pub.10.1007/s00775-013-1025-1'

N-Triples is a line-based linked data format ideal for batch operations.

curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1007/s00775-013-1025-1'

Turtle is a human-readable linked data format.

curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1007/s00775-013-1025-1'

RDF/XML is a standard XML format for linked data.

curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1007/s00775-013-1025-1'


 

This table displays all metadata directly associated to this object as RDF triples.

271 TRIPLES      21 PREDICATES      114 URIs      101 LITERALS      19 BLANK NODES

Subject Predicate Object
1 sg:pub.10.1007/s00775-013-1025-1 schema:about N132b62a143b6456e93fd7b3a32e2b52a
2 N6a74c772695d492e89beec22abb206bb
3 N7c24010017234cda9e8ab04af4f722b8
4 N8a82097d84bb4afc82a644992ba546e3
5 N8bda969f29fe485a840fb96c463418f0
6 N9a76e805098a4fb1ada56f8a7bf1207e
7 Na0e0c7bbe8264809a8185daae5167ab8
8 Nb0328df218c141de9c7afe8e41d0277b
9 Nd0dc1b74cfb141b8b00e7cfabd54908f
10 Nd1696ffc09124a668283310ead988912
11 Nd250ddd63c3a483499b72df64f3f738a
12 Nde4a95592fc14f3292dfdd3a297dba0c
13 anzsrc-for:03
14 anzsrc-for:0306
15 schema:author Nd599d809719c4cfaabb54db370ade331
16 schema:citation sg:pub.10.1007/s00775-003-0465-4
17 sg:pub.10.1007/s00775-006-0104-y
18 sg:pub.10.1007/s007750050064
19 sg:pub.10.1007/s007750050184
20 sg:pub.10.1038/nchembio.85
21 schema:datePublished 2013-08-06
22 schema:datePublishedReg 2013-08-06
23 schema:description Superoxide reductase (SOR) is a non-heme iron metalloenzyme that detoxifies superoxide radical in microorganisms. Its active site consists of an unusual non-heme Fe2+ center in a [His4Cys1] square pyramidal pentacoordination, with the axial cysteine ligand proposed to be an essential feature in catalysis. Two NH peptide groups from isoleucine 118 and histidine 119 establish hydrogen bonds involving the sulfur ligand (Desulfoarculus baarsii SOR numbering). To investigate the catalytic role of these hydrogen bonds, the isoleucine 118 residue of the SOR from Desulfoarculus baarsii was mutated into alanine, aspartate, or serine residues. Resonance Raman spectroscopy showed that the mutations specifically induced an increase of the strength of the Fe3+–S(Cys) and S–Cβ(Cys) bonds as well as a change in conformation of the cysteinyl side chain, which was associated with the alteration of the NH hydrogen bonding involving the sulfur ligand. The effects of the isoleucine mutations on the reactivity of SOR with O2•− were investigated by pulse radiolysis. These studies showed that the mutations induced a specific increase of the pKa of the first reaction intermediate, recently proposed to be an Fe2+–O2•− species. These data were supported by density functional theory calculations conducted on three models of the Fe2+–O2•− intermediate, with one, two, or no hydrogen bonds involving the sulfur ligand. Our results demonstrated that the hydrogen bonds between the NH (peptide) and the cysteine ligand tightly control the rate of protonation of the Fe2+–O2•− reaction intermediate to form an Fe3+–OOH species.
24 schema:genre article
25 schema:isAccessibleForFree true
26 schema:isPartOf N437cfc20d4bc4f52ac5b381d9251e3d8
27 N4f6c1a3398d749f78adb07b1a534acee
28 sg:journal.1116242
29 schema:keywords Desulfoarculus baarsii
30 Fe2
31 NH
32 NH hydrogen bonding
33 OOH species
34 Raman spectroscopy
35 SOR
36 acid-base control
37 active site
38 alanine
39 alterations
40 aspartate
41 axial cysteine ligand
42 bonding
43 bonds
44 calculations
45 catalysis
46 catalytic role
47 center
48 chain
49 changes
50 conformation
51 control
52 cysteine ligands
53 cysteinyl side chains
54 data
55 density functional theory calculations
56 detoxifies
57 effect
58 essential features
59 features
60 first reaction intermediate
61 functional theory calculations
62 group
63 hydrogen bonding
64 hydrogen bonds
65 increase
66 intermediates
67 iron metalloenzyme
68 isoleucine mutation
69 ligands
70 metalloenzymes
71 microorganisms
72 model
73 mutations
74 non-heme Fe2
75 pentacoordination
76 peptide groups
77 protonation
78 pulse radiolysis
79 radiolysis
80 rate
81 rate of protonation
82 reaction
83 reaction intermediates
84 reactivity
85 reductase
86 residues
87 resonance Raman spectroscopy
88 results
89 role
90 serine residues
91 side chains
92 sites
93 species
94 specific increase
95 spectroscopy
96 strength
97 study
98 sulfur ligands
99 superoxide reductase
100 theory calculations
101 schema:name Hydrogen bonding to the cysteine ligand of superoxide reductase: acid–base control of the reaction intermediates
102 schema:pagination 815-830
103 schema:productId N3b848d77ee0d4fdeb355064129a23566
104 N5f598cef5c5b4f5eb94ee90d23a15175
105 Ne85b48d3cc404ea5aaa76454e84e9a2b
106 schema:sameAs https://app.dimensions.ai/details/publication/pub.1038119476
107 https://doi.org/10.1007/s00775-013-1025-1
108 schema:sdDatePublished 2022-10-01T06:38
109 schema:sdLicense https://scigraph.springernature.com/explorer/license/
110 schema:sdPublisher N2a74821c73e945e8b527a32a48ff71e8
111 schema:url https://doi.org/10.1007/s00775-013-1025-1
112 sgo:license sg:explorer/license/
113 sgo:sdDataset articles
114 rdf:type schema:ScholarlyArticle
115 N132b62a143b6456e93fd7b3a32e2b52a schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
116 schema:name Hydrogen Bonding
117 rdf:type schema:DefinedTerm
118 N2a74821c73e945e8b527a32a48ff71e8 schema:name Springer Nature - SN SciGraph project
119 rdf:type schema:Organization
120 N3b848d77ee0d4fdeb355064129a23566 schema:name dimensions_id
121 schema:value pub.1038119476
122 rdf:type schema:PropertyValue
123 N437cfc20d4bc4f52ac5b381d9251e3d8 schema:issueNumber 7
124 rdf:type schema:PublicationIssue
125 N4f6c1a3398d749f78adb07b1a534acee schema:volumeNumber 18
126 rdf:type schema:PublicationVolume
127 N5f598cef5c5b4f5eb94ee90d23a15175 schema:name pubmed_id
128 schema:value 23917995
129 rdf:type schema:PropertyValue
130 N6a74c772695d492e89beec22abb206bb schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
131 schema:name Catalytic Domain
132 rdf:type schema:DefinedTerm
133 N7c24010017234cda9e8ab04af4f722b8 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
134 schema:name Ligands
135 rdf:type schema:DefinedTerm
136 N820b2608726d4a0a90f6d41480e0766c rdf:first sg:person.01021251511.66
137 rdf:rest Nf75b7b003fd3427390a2ab053dffdc03
138 N8a82097d84bb4afc82a644992ba546e3 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
139 schema:name Proteobacteria
140 rdf:type schema:DefinedTerm
141 N8bda969f29fe485a840fb96c463418f0 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
142 schema:name Models, Molecular
143 rdf:type schema:DefinedTerm
144 N8d51fa2f73a74fa5a53680177cc576d5 rdf:first sg:person.01203613311.33
145 rdf:rest Nb0907e5b0e814eaaadc7c1b22dae5c38
146 N9a76e805098a4fb1ada56f8a7bf1207e schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
147 schema:name Mutation
148 rdf:type schema:DefinedTerm
149 Na0e0c7bbe8264809a8185daae5167ab8 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
150 schema:name Mutagenesis, Site-Directed
151 rdf:type schema:DefinedTerm
152 Na3b0278e8726459fba0f77d390c56d93 rdf:first sg:person.0636707711.52
153 rdf:rest N820b2608726d4a0a90f6d41480e0766c
154 Na5fe4c74306a4911baa1e03f3b63130b rdf:first sg:person.01216650776.59
155 rdf:rest Nca6becedafa34bbd9b2ef71495a3e1a0
156 Na68debc2b31e4d14bad82b96a6cf001c rdf:first sg:person.0657101562.93
157 rdf:rest N8d51fa2f73a74fa5a53680177cc576d5
158 Nb0328df218c141de9c7afe8e41d0277b schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
159 schema:name Oxidoreductases
160 rdf:type schema:DefinedTerm
161 Nb0907e5b0e814eaaadc7c1b22dae5c38 rdf:first sg:person.01044625215.48
162 rdf:rest rdf:nil
163 Nca6becedafa34bbd9b2ef71495a3e1a0 rdf:first sg:person.071237417.08
164 rdf:rest Na68debc2b31e4d14bad82b96a6cf001c
165 Nd0dc1b74cfb141b8b00e7cfabd54908f schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
166 schema:name Hydrogen-Ion Concentration
167 rdf:type schema:DefinedTerm
168 Nd1696ffc09124a668283310ead988912 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
169 schema:name Cysteine
170 rdf:type schema:DefinedTerm
171 Nd250ddd63c3a483499b72df64f3f738a schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
172 schema:name Oxidation-Reduction
173 rdf:type schema:DefinedTerm
174 Nd599d809719c4cfaabb54db370ade331 rdf:first sg:person.01307624625.23
175 rdf:rest Na3b0278e8726459fba0f77d390c56d93
176 Nde4a95592fc14f3292dfdd3a297dba0c schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
177 schema:name Quantum Theory
178 rdf:type schema:DefinedTerm
179 Ne85b48d3cc404ea5aaa76454e84e9a2b schema:name doi
180 schema:value 10.1007/s00775-013-1025-1
181 rdf:type schema:PropertyValue
182 Nf75b7b003fd3427390a2ab053dffdc03 rdf:first sg:person.0641716334.91
183 rdf:rest Na5fe4c74306a4911baa1e03f3b63130b
184 anzsrc-for:03 schema:inDefinedTermSet anzsrc-for:
185 schema:name Chemical Sciences
186 rdf:type schema:DefinedTerm
187 anzsrc-for:0306 schema:inDefinedTermSet anzsrc-for:
188 schema:name Physical Chemistry (incl. Structural)
189 rdf:type schema:DefinedTerm
190 sg:journal.1116242 schema:issn 0949-8257
191 1432-1327
192 schema:name JBIC Journal of Biological Inorganic Chemistry
193 schema:publisher Springer Nature
194 rdf:type schema:Periodical
195 sg:person.01021251511.66 schema:affiliation grid-institutes:grid.9621.c
196 schema:familyName Moreau
197 schema:givenName Yohann
198 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01021251511.66
199 rdf:type schema:Person
200 sg:person.01044625215.48 schema:affiliation grid-institutes:grid.9621.c
201 schema:familyName Nivière
202 schema:givenName Vincent
203 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01044625215.48
204 rdf:type schema:Person
205 sg:person.01203613311.33 schema:affiliation grid-institutes:grid.462861.f
206 schema:familyName Houée-Levin
207 schema:givenName Chantal
208 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01203613311.33
209 rdf:type schema:Person
210 sg:person.01216650776.59 schema:affiliation grid-institutes:grid.457334.2
211 schema:familyName Desbois
212 schema:givenName Alain
213 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01216650776.59
214 rdf:type schema:Person
215 sg:person.01307624625.23 schema:affiliation grid-institutes:grid.9621.c
216 schema:familyName Tremey
217 schema:givenName Emilie
218 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01307624625.23
219 rdf:type schema:Person
220 sg:person.0636707711.52 schema:affiliation grid-institutes:grid.9621.c
221 schema:familyName Bonnot
222 schema:givenName Florence
223 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0636707711.52
224 rdf:type schema:Person
225 sg:person.0641716334.91 schema:affiliation grid-institutes:grid.5399.6
226 schema:familyName Berthomieu
227 schema:givenName Catherine
228 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0641716334.91
229 rdf:type schema:Person
230 sg:person.0657101562.93 schema:affiliation grid-institutes:grid.9621.c
231 schema:familyName Blondin
232 schema:givenName Geneviève
233 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0657101562.93
234 rdf:type schema:Person
235 sg:person.071237417.08 schema:affiliation grid-institutes:grid.5842.b
236 schema:familyName Favaudon
237 schema:givenName Vincent
238 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.071237417.08
239 rdf:type schema:Person
240 sg:pub.10.1007/s00775-003-0465-4 schema:sameAs https://app.dimensions.ai/details/publication/pub.1023330125
241 https://doi.org/10.1007/s00775-003-0465-4
242 rdf:type schema:CreativeWork
243 sg:pub.10.1007/s00775-006-0104-y schema:sameAs https://app.dimensions.ai/details/publication/pub.1010325438
244 https://doi.org/10.1007/s00775-006-0104-y
245 rdf:type schema:CreativeWork
246 sg:pub.10.1007/s007750050064 schema:sameAs https://app.dimensions.ai/details/publication/pub.1041779936
247 https://doi.org/10.1007/s007750050064
248 rdf:type schema:CreativeWork
249 sg:pub.10.1007/s007750050184 schema:sameAs https://app.dimensions.ai/details/publication/pub.1027260643
250 https://doi.org/10.1007/s007750050184
251 rdf:type schema:CreativeWork
252 sg:pub.10.1038/nchembio.85 schema:sameAs https://app.dimensions.ai/details/publication/pub.1021452802
253 https://doi.org/10.1038/nchembio.85
254 rdf:type schema:CreativeWork
255 grid-institutes:grid.457334.2 schema:alternateName Laboratoire Stress Oxydant et Détoxication, SB2SM and CNRS UMR 8221, iBiTec-S, CEA Saclay, 91191, Gif-sur-Yvette Cedex, France
256 schema:name Laboratoire Stress Oxydant et Détoxication, SB2SM and CNRS UMR 8221, iBiTec-S, CEA Saclay, 91191, Gif-sur-Yvette Cedex, France
257 rdf:type schema:Organization
258 grid-institutes:grid.462861.f schema:alternateName Laboratoire de Chimie Physique, CNRS/Université Paris-Sud, Bâtiment 350, Centre Universitaire, 91405, Orsay Cedex, France
259 schema:name Laboratoire de Chimie Physique, CNRS/Université Paris-Sud, Bâtiment 350, Centre Universitaire, 91405, Orsay Cedex, France
260 rdf:type schema:Organization
261 grid-institutes:grid.5399.6 schema:alternateName Laboratoire Des Interactions Protéine Métal, SBVME-CEA Cadarache/CNRS/Université Aix-Marseille II, 13108, Saint-Paul-lez-Durance Cedex, France
262 schema:name Laboratoire Des Interactions Protéine Métal, SBVME-CEA Cadarache/CNRS/Université Aix-Marseille II, 13108, Saint-Paul-lez-Durance Cedex, France
263 rdf:type schema:Organization
264 grid-institutes:grid.5842.b schema:alternateName Inserm Unité 612 and Institut Curie, Bâtiment 110-112, Centre Universitaire, 91405, Orsay Cedex, France
265 schema:name Inserm Unité 612 and Institut Curie, Bâtiment 110-112, Centre Universitaire, 91405, Orsay Cedex, France
266 rdf:type schema:Organization
267 grid-institutes:grid.9621.c schema:alternateName Université de Grenoble, 38000, Grenoble, France
268 schema:name CNRS, UMR 5249, 38054, Grenoble, France
269 Laboratoire de Chimie et Biologie des Métaux, CEA, iRTSV, 17 avenue des Martyrs, 38054, Grenoble, France
270 Université de Grenoble, 38000, Grenoble, France
271 rdf:type schema:Organization
 




Preview window. Press ESC to close (or click here)


...