Modulation of the flavin-protein interactions in NADH peroxidase and mercuric ion reductase: a resonance Raman study.
Identifieur interne : 000604 ( PubMed/Curation ); précédent : 000603; suivant : 000605Modulation of the flavin-protein interactions in NADH peroxidase and mercuric ion reductase: a resonance Raman study.
Auteurs : Julie Keirsse-Haquin [France] ; Thierry Picaud [France] ; Luc Bordes [France] ; Adrienne Gomez De Gracia [France] ; Alain Desbois [France]Source :
- European biophysics journal : EBJ [ 1432-1017 ] ; 2017.
Abstract
NADH peroxidase (Npx) and mercuric ion reductase (MerA) are flavoproteins belonging to the pyridine nucleotide:disulfide oxidoreductases (PNDO) and catalyzing the reduction of toxic substrates, i.e., hydrogen peroxide and mercuric ion, respectively. To determine the role of the flavin adenine dinucleotide (FAD) in the detoxification mechanism, the resonance Raman (RR) spectra of these enzymes under various redox and ligation states have been investigated using blue and/or near-UV excitation(s). These data were compared to those previously obtained for glutathione reductase (GR), another enzyme of the PNDO family, but catalyzing the reduction of oxidized glutathione. Spectral differences have been detected for the marker bands of the isoalloxazine ring of Npx, MerA, and GR. They provide evidence for different catalytic mechanisms in these flavoproteins. The RR modes of the oxidized and two-electron reduced (EH2) forms of Npx are related to very tight flavin-protein interactions maintaining a nearly planar conformation of the isoalloxazine tricycle, a low level of H-bonding at the N1/N5 and O2/O4 sites, and a strong H-bond at N3H. They also indicate minimal changes in FAD structure and environment upon either NAD(H) binding or reduction of the sulfinic redox center. All these spectroscopic data support an enzyme functioning centered on the Cys-SO(-)/Cys-S(-) redox moiety and a neighbouring His residue. On the contrary, the RR data on various functional forms of MerA are indicative of a modulation of both ring II distortion and H-bonding states of the N5 site and ring III. The Cd(II) binding to the EH2-NADP(H) complexes, biomimetic intermediates in the reaction of Hg(II) reduction, provokes important spectral changes. They are interpreted in terms of flattening of the isoalloxazine ring and large decreases in H-bonding at the N5 site and ring III. The large flexibility of the FAD structure and environment in MerA is in agreement with proposed mechanisms involving C4a(flavin) adducts.
DOI: 10.1007/s00249-017-1245-3
PubMed: 28889232
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: Pour aller vers cette notice dans l'étape Curation :000606
Links to Exploration step
pubmed:28889232Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Modulation of the flavin-protein interactions in NADH peroxidase and mercuric ion reductase: a resonance Raman study.</title>
<author><name sortKey="Keirsse Haquin, Julie" sort="Keirsse Haquin, Julie" uniqKey="Keirsse Haquin J" first="Julie" last="Keirsse-Haquin">Julie Keirsse-Haquin</name>
<affiliation wicri:level="1"><nlm:affiliation>Institut de Biologie Intégrative de la Cellule, UMR 9198 CNRS-CEA-Université Paris Sud, CEA Saclay, 91191, Gif-sur-Yvette Cedex, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Institut de Biologie Intégrative de la Cellule, UMR 9198 CNRS-CEA-Université Paris Sud, CEA Saclay, 91191, Gif-sur-Yvette Cedex</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Picaud, Thierry" sort="Picaud, Thierry" uniqKey="Picaud T" first="Thierry" last="Picaud">Thierry Picaud</name>
<affiliation wicri:level="1"><nlm:affiliation>Institut de Biologie Intégrative de la Cellule, UMR 9198 CNRS-CEA-Université Paris Sud, CEA Saclay, 91191, Gif-sur-Yvette Cedex, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Institut de Biologie Intégrative de la Cellule, UMR 9198 CNRS-CEA-Université Paris Sud, CEA Saclay, 91191, Gif-sur-Yvette Cedex</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Bordes, Luc" sort="Bordes, Luc" uniqKey="Bordes L" first="Luc" last="Bordes">Luc Bordes</name>
<affiliation wicri:level="1"><nlm:affiliation>Institut de Biologie Intégrative de la Cellule, UMR 9198 CNRS-CEA-Université Paris Sud, CEA Saclay, 91191, Gif-sur-Yvette Cedex, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Institut de Biologie Intégrative de la Cellule, UMR 9198 CNRS-CEA-Université Paris Sud, CEA Saclay, 91191, Gif-sur-Yvette Cedex</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="De Gracia, Adrienne Gomez" sort="De Gracia, Adrienne Gomez" uniqKey="De Gracia A" first="Adrienne Gomez" last="De Gracia">Adrienne Gomez De Gracia</name>
<affiliation wicri:level="1"><nlm:affiliation>Institut de Biologie Intégrative de la Cellule, UMR 9198 CNRS-CEA-Université Paris Sud, CEA Saclay, 91191, Gif-sur-Yvette Cedex, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Institut de Biologie Intégrative de la Cellule, UMR 9198 CNRS-CEA-Université Paris Sud, CEA Saclay, 91191, Gif-sur-Yvette Cedex</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Desbois, Alain" sort="Desbois, Alain" uniqKey="Desbois A" first="Alain" last="Desbois">Alain Desbois</name>
<affiliation wicri:level="1"><nlm:affiliation>Institut de Biologie Intégrative de la Cellule, UMR 9198 CNRS-CEA-Université Paris Sud, CEA Saclay, 91191, Gif-sur-Yvette Cedex, France. alain.desbois@cea.fr.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Institut de Biologie Intégrative de la Cellule, UMR 9198 CNRS-CEA-Université Paris Sud, CEA Saclay, 91191, Gif-sur-Yvette Cedex</wicri:regionArea>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2017">2017</date>
<idno type="RBID">pubmed:28889232</idno>
<idno type="pmid">28889232</idno>
<idno type="doi">10.1007/s00249-017-1245-3</idno>
<idno type="wicri:Area/PubMed/Corpus">000606</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000606</idno>
<idno type="wicri:Area/PubMed/Curation">000604</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000604</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Modulation of the flavin-protein interactions in NADH peroxidase and mercuric ion reductase: a resonance Raman study.</title>
<author><name sortKey="Keirsse Haquin, Julie" sort="Keirsse Haquin, Julie" uniqKey="Keirsse Haquin J" first="Julie" last="Keirsse-Haquin">Julie Keirsse-Haquin</name>
<affiliation wicri:level="1"><nlm:affiliation>Institut de Biologie Intégrative de la Cellule, UMR 9198 CNRS-CEA-Université Paris Sud, CEA Saclay, 91191, Gif-sur-Yvette Cedex, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Institut de Biologie Intégrative de la Cellule, UMR 9198 CNRS-CEA-Université Paris Sud, CEA Saclay, 91191, Gif-sur-Yvette Cedex</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Picaud, Thierry" sort="Picaud, Thierry" uniqKey="Picaud T" first="Thierry" last="Picaud">Thierry Picaud</name>
<affiliation wicri:level="1"><nlm:affiliation>Institut de Biologie Intégrative de la Cellule, UMR 9198 CNRS-CEA-Université Paris Sud, CEA Saclay, 91191, Gif-sur-Yvette Cedex, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Institut de Biologie Intégrative de la Cellule, UMR 9198 CNRS-CEA-Université Paris Sud, CEA Saclay, 91191, Gif-sur-Yvette Cedex</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Bordes, Luc" sort="Bordes, Luc" uniqKey="Bordes L" first="Luc" last="Bordes">Luc Bordes</name>
<affiliation wicri:level="1"><nlm:affiliation>Institut de Biologie Intégrative de la Cellule, UMR 9198 CNRS-CEA-Université Paris Sud, CEA Saclay, 91191, Gif-sur-Yvette Cedex, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Institut de Biologie Intégrative de la Cellule, UMR 9198 CNRS-CEA-Université Paris Sud, CEA Saclay, 91191, Gif-sur-Yvette Cedex</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="De Gracia, Adrienne Gomez" sort="De Gracia, Adrienne Gomez" uniqKey="De Gracia A" first="Adrienne Gomez" last="De Gracia">Adrienne Gomez De Gracia</name>
<affiliation wicri:level="1"><nlm:affiliation>Institut de Biologie Intégrative de la Cellule, UMR 9198 CNRS-CEA-Université Paris Sud, CEA Saclay, 91191, Gif-sur-Yvette Cedex, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Institut de Biologie Intégrative de la Cellule, UMR 9198 CNRS-CEA-Université Paris Sud, CEA Saclay, 91191, Gif-sur-Yvette Cedex</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Desbois, Alain" sort="Desbois, Alain" uniqKey="Desbois A" first="Alain" last="Desbois">Alain Desbois</name>
<affiliation wicri:level="1"><nlm:affiliation>Institut de Biologie Intégrative de la Cellule, UMR 9198 CNRS-CEA-Université Paris Sud, CEA Saclay, 91191, Gif-sur-Yvette Cedex, France. alain.desbois@cea.fr.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Institut de Biologie Intégrative de la Cellule, UMR 9198 CNRS-CEA-Université Paris Sud, CEA Saclay, 91191, Gif-sur-Yvette Cedex</wicri:regionArea>
</affiliation>
</author>
</analytic>
<series><title level="j">European biophysics journal : EBJ</title>
<idno type="eISSN">1432-1017</idno>
<imprint><date when="2017" type="published">2017</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass></textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">NADH peroxidase (Npx) and mercuric ion reductase (MerA) are flavoproteins belonging to the pyridine nucleotide:disulfide oxidoreductases (PNDO) and catalyzing the reduction of toxic substrates, i.e., hydrogen peroxide and mercuric ion, respectively. To determine the role of the flavin adenine dinucleotide (FAD) in the detoxification mechanism, the resonance Raman (RR) spectra of these enzymes under various redox and ligation states have been investigated using blue and/or near-UV excitation(s). These data were compared to those previously obtained for glutathione reductase (GR), another enzyme of the PNDO family, but catalyzing the reduction of oxidized glutathione. Spectral differences have been detected for the marker bands of the isoalloxazine ring of Npx, MerA, and GR. They provide evidence for different catalytic mechanisms in these flavoproteins. The RR modes of the oxidized and two-electron reduced (EH2) forms of Npx are related to very tight flavin-protein interactions maintaining a nearly planar conformation of the isoalloxazine tricycle, a low level of H-bonding at the N1/N5 and O2/O4 sites, and a strong H-bond at N3H. They also indicate minimal changes in FAD structure and environment upon either NAD(H) binding or reduction of the sulfinic redox center. All these spectroscopic data support an enzyme functioning centered on the Cys-SO(-)/Cys-S(-) redox moiety and a neighbouring His residue. On the contrary, the RR data on various functional forms of MerA are indicative of a modulation of both ring II distortion and H-bonding states of the N5 site and ring III. The Cd(II) binding to the EH2-NADP(H) complexes, biomimetic intermediates in the reaction of Hg(II) reduction, provokes important spectral changes. They are interpreted in terms of flattening of the isoalloxazine ring and large decreases in H-bonding at the N5 site and ring III. The large flexibility of the FAD structure and environment in MerA is in agreement with proposed mechanisms involving C4a(flavin) adducts.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">28889232</PMID>
<DateCreated><Year>2017</Year>
<Month>09</Month>
<Day>10</Day>
</DateCreated>
<DateRevised><Year>2017</Year>
<Month>09</Month>
<Day>10</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1432-1017</ISSN>
<JournalIssue CitedMedium="Internet"><PubDate><Year>2017</Year>
<Month>Sep</Month>
<Day>09</Day>
</PubDate>
</JournalIssue>
<Title>European biophysics journal : EBJ</Title>
<ISOAbbreviation>Eur. Biophys. J.</ISOAbbreviation>
</Journal>
<ArticleTitle>Modulation of the flavin-protein interactions in NADH peroxidase and mercuric ion reductase: a resonance Raman study.</ArticleTitle>
<ELocationID EIdType="doi" ValidYN="Y">10.1007/s00249-017-1245-3</ELocationID>
<Abstract><AbstractText>NADH peroxidase (Npx) and mercuric ion reductase (MerA) are flavoproteins belonging to the pyridine nucleotide:disulfide oxidoreductases (PNDO) and catalyzing the reduction of toxic substrates, i.e., hydrogen peroxide and mercuric ion, respectively. To determine the role of the flavin adenine dinucleotide (FAD) in the detoxification mechanism, the resonance Raman (RR) spectra of these enzymes under various redox and ligation states have been investigated using blue and/or near-UV excitation(s). These data were compared to those previously obtained for glutathione reductase (GR), another enzyme of the PNDO family, but catalyzing the reduction of oxidized glutathione. Spectral differences have been detected for the marker bands of the isoalloxazine ring of Npx, MerA, and GR. They provide evidence for different catalytic mechanisms in these flavoproteins. The RR modes of the oxidized and two-electron reduced (EH2) forms of Npx are related to very tight flavin-protein interactions maintaining a nearly planar conformation of the isoalloxazine tricycle, a low level of H-bonding at the N1/N5 and O2/O4 sites, and a strong H-bond at N3H. They also indicate minimal changes in FAD structure and environment upon either NAD(H) binding or reduction of the sulfinic redox center. All these spectroscopic data support an enzyme functioning centered on the Cys-SO(-)/Cys-S(-) redox moiety and a neighbouring His residue. On the contrary, the RR data on various functional forms of MerA are indicative of a modulation of both ring II distortion and H-bonding states of the N5 site and ring III. The Cd(II) binding to the EH2-NADP(H) complexes, biomimetic intermediates in the reaction of Hg(II) reduction, provokes important spectral changes. They are interpreted in terms of flattening of the isoalloxazine ring and large decreases in H-bonding at the N5 site and ring III. The large flexibility of the FAD structure and environment in MerA is in agreement with proposed mechanisms involving C4a(flavin) adducts.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Keirsse-Haquin</LastName>
<ForeName>Julie</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Institut de Biologie Intégrative de la Cellule, UMR 9198 CNRS-CEA-Université Paris Sud, CEA Saclay, 91191, Gif-sur-Yvette Cedex, France.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Ecole Nationale Supérieure des Mines, 44300, Nantes, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Picaud</LastName>
<ForeName>Thierry</ForeName>
<Initials>T</Initials>
<AffiliationInfo><Affiliation>Institut de Biologie Intégrative de la Cellule, UMR 9198 CNRS-CEA-Université Paris Sud, CEA Saclay, 91191, Gif-sur-Yvette Cedex, France.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Institut Supérieur des Biotechnologies de Paris (Sup'Biotech Paris), 94800, Villejuif, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Bordes</LastName>
<ForeName>Luc</ForeName>
<Initials>L</Initials>
<AffiliationInfo><Affiliation>Institut de Biologie Intégrative de la Cellule, UMR 9198 CNRS-CEA-Université Paris Sud, CEA Saclay, 91191, Gif-sur-Yvette Cedex, France.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>School of Earth and Environmental Sciences, University of Wollongong, Wollongong, NSW, 2522, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>de Gracia</LastName>
<ForeName>Adrienne Gomez</ForeName>
<Initials>AG</Initials>
<AffiliationInfo><Affiliation>Institut de Biologie Intégrative de la Cellule, UMR 9198 CNRS-CEA-Université Paris Sud, CEA Saclay, 91191, Gif-sur-Yvette Cedex, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Desbois</LastName>
<ForeName>Alain</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>Institut de Biologie Intégrative de la Cellule, UMR 9198 CNRS-CEA-Université Paris Sud, CEA Saclay, 91191, Gif-sur-Yvette Cedex, France. alain.desbois@cea.fr.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2017</Year>
<Month>09</Month>
<Day>09</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>Germany</Country>
<MedlineTA>Eur Biophys J</MedlineTA>
<NlmUniqueID>8409413</NlmUniqueID>
<ISSNLinking>0175-7571</ISSNLinking>
</MedlineJournalInfo>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Detoxification mechanism</Keyword>
<Keyword MajorTopicYN="N">Flavin–protein interactions</Keyword>
<Keyword MajorTopicYN="N">Isoalloxazine modes</Keyword>
<Keyword MajorTopicYN="N">Resonance Raman</Keyword>
</KeywordList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year>
<Month>05</Month>
<Day>15</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2017</Year>
<Month>07</Month>
<Day>26</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised"><Year>2017</Year>
<Month>07</Month>
<Day>12</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2017</Year>
<Month>9</Month>
<Day>11</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2017</Year>
<Month>9</Month>
<Day>11</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2017</Year>
<Month>9</Month>
<Day>11</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>aheadofprint</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">28889232</ArticleId>
<ArticleId IdType="doi">10.1007/s00249-017-1245-3</ArticleId>
<ArticleId IdType="pii">10.1007/s00249-017-1245-3</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Asie/explor/AustralieFrV1/Data/PubMed/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000604 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd -nk 000604 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Wicri/Asie |area= AustralieFrV1 |flux= PubMed |étape= Curation |type= RBID |clé= pubmed:28889232 |texte= Modulation of the flavin-protein interactions in NADH peroxidase and mercuric ion reductase: a resonance Raman study. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Curation/RBID.i -Sk "pubmed:28889232" \ | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd \ | NlmPubMed2Wicri -a AustralieFrV1
![]() | This area was generated with Dilib version V0.6.33. | ![]() |