DetoxFungiV1, Main, Exploration, bibRecord, 002205

Structural and functional properties of a single domain hemoglobin from the food-borne pathogen Campylobactor jejuni.

Identifieur interne : 002205 ( Main/Exploration ); précédent : 002204; suivant : 002206

Structural and functional properties of a single domain hemoglobin from the food-borne pathogen Campylobactor jejuni.

Auteurs : Changyuan Lu [États-Unis] ; Masahiro Mukai ; Yu Lin ; Guanghui Wu ; Robert K. Poole ; Syun-Ru Yeh

Source :

The Journal of biological chemistry [ 0021-9258 ] ; 2007.

RBID : pubmed:17606611

Descripteurs français

English descriptors

KwdEn :
- Amino Acids (chemistry), Amino Acids (metabolism), Bacterial Proteins (MeSH), Binding Sites (MeSH), Campylobacter jejuni (chemistry), Campylobacter jejuni (metabolism), Catalysis (MeSH), Food Microbiology (MeSH), Hemoglobins (chemistry), Hemoglobins (metabolism), Hydrogen Bonding (MeSH), Nitric Oxide (chemistry), Nitric Oxide (metabolism), Oxygen (chemistry), Oxygen (metabolism), Spectrum Analysis, Raman (MeSH), Structure-Activity Relationship (MeSH), Truncated Hemoglobins (MeSH).
MESH :
- chemical , chemistry : Amino Acids, Hemoglobins, Nitric Oxide, Oxygen.
- chemical , metabolism : Amino Acids, Hemoglobins, Nitric Oxide, Oxygen.
- chemical : Bacterial Proteins, Truncated Hemoglobins.
- chemistry : Campylobacter jejuni.
- metabolism : Campylobacter jejuni.
- Binding Sites, Catalysis, Food Microbiology, Hydrogen Bonding, Spectrum Analysis, Raman, Structure-Activity Relationship.

Abstract

Campylobacter jejuni contains two globins, a truncated hemoglobin, Ctb, and a single domain hemoglobin, Cgb. The physiological function of Ctb remains unclear, whereas Cgb has been linked to NO detoxification. With resonance Raman scattering, the iron-histidine stretching mode of Cgb was identified at 251 cm(-1). This frequency is unusually high, suggesting an imidazolate character of the proximal histidine as a result of the H-bonding network linking the catalytic triad involving the F8His, H23Glu, and G5Tyr residues. In the CO-complex, two conformers were identified with the nuC-O/nuFe-CO at 529/1914 cm(-1) and 492/1963 cm(-1). The former is assigned to a "closed" conformation, in which the heme-bound CO is stabilized by the H-bond(s) donated from the B10Tyr-E7Gln residues, whereas the latter is assigned to an "open" conformer, in which the H-bonding interaction is absent. The presence of the two alternative conformations demonstrates the plasticity of the protein matrix. In the O2-complex, the iron-O2 stretching frequency was identified at 554 cm(-1), which is unusually low, indicating that the heme-bound O2 is stabilized by strong H-bond(s) donated by the B10Tyr-E7Gln residues. This scenario is consistent with its low O2 off-rate (0.87 s(-1)). Taken together the data suggest that the NO-detoxifying activity of Cgb is facilitated by the imidazolate character of the proximal F8His and the distal positive polar environment provided by the B10Tyr-E7Gln. They may offer electronic "push" and "pull," respectively, for the O-O bond cleavage reaction required for the isomerization of the presumed peroxynitrite intermediate to the product, nitrate.

DOI: 10.1074/jbc.M704415200
PubMed: 17606611

Affiliations:

États-Unis

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 002224
to stream Main, to step Curation: 002224

Le document en format XML

<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Structural and functional properties of a single domain hemoglobin from the food-borne pathogen Campylobactor jejuni.</title>
<author><name sortKey="Lu, Changyuan" sort="Lu, Changyuan" uniqKey="Lu C" first="Changyuan" last="Lu">Changyuan Lu</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461</wicri:regionArea>
<wicri:noRegion>New York 10461</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Mukai, Masahiro" sort="Mukai, Masahiro" uniqKey="Mukai M" first="Masahiro" last="Mukai">Masahiro Mukai</name>
</author>
<author><name sortKey="Lin, Yu" sort="Lin, Yu" uniqKey="Lin Y" first="Yu" last="Lin">Yu Lin</name>
</author>
<author><name sortKey="Wu, Guanghui" sort="Wu, Guanghui" uniqKey="Wu G" first="Guanghui" last="Wu">Guanghui Wu</name>
</author>
<author><name sortKey="Poole, Robert K" sort="Poole, Robert K" uniqKey="Poole R" first="Robert K" last="Poole">Robert K. Poole</name>
</author>
<author><name sortKey="Yeh, Syun Ru" sort="Yeh, Syun Ru" uniqKey="Yeh S" first="Syun-Ru" last="Yeh">Syun-Ru Yeh</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2007">2007</date>
<idno type="RBID">pubmed:17606611</idno>
<idno type="pmid">17606611</idno>
<idno type="doi">10.1074/jbc.M704415200</idno>
<idno type="wicri:Area/Main/Corpus">002224</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002224</idno>
<idno type="wicri:Area/Main/Curation">002224</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">002224</idno>
<idno type="wicri:Area/Main/Exploration">002224</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Structural and functional properties of a single domain hemoglobin from the food-borne pathogen Campylobactor jejuni.</title>
<author><name sortKey="Lu, Changyuan" sort="Lu, Changyuan" uniqKey="Lu C" first="Changyuan" last="Lu">Changyuan Lu</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461</wicri:regionArea>
<wicri:noRegion>New York 10461</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Mukai, Masahiro" sort="Mukai, Masahiro" uniqKey="Mukai M" first="Masahiro" last="Mukai">Masahiro Mukai</name>
</author>
<author><name sortKey="Lin, Yu" sort="Lin, Yu" uniqKey="Lin Y" first="Yu" last="Lin">Yu Lin</name>
</author>
<author><name sortKey="Wu, Guanghui" sort="Wu, Guanghui" uniqKey="Wu G" first="Guanghui" last="Wu">Guanghui Wu</name>
</author>
<author><name sortKey="Poole, Robert K" sort="Poole, Robert K" uniqKey="Poole R" first="Robert K" last="Poole">Robert K. Poole</name>
</author>
<author><name sortKey="Yeh, Syun Ru" sort="Yeh, Syun Ru" uniqKey="Yeh S" first="Syun-Ru" last="Yeh">Syun-Ru Yeh</name>
</author>
</analytic>
<series><title level="j">The Journal of biological chemistry</title>
<idno type="ISSN">0021-9258</idno>
<imprint><date when="2007" type="published">2007</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acids (chemistry)</term>
<term>Amino Acids (metabolism)</term>
<term>Bacterial Proteins (MeSH)</term>
<term>Binding Sites (MeSH)</term>
<term>Campylobacter jejuni (chemistry)</term>
<term>Campylobacter jejuni (metabolism)</term>
<term>Catalysis (MeSH)</term>
<term>Food Microbiology (MeSH)</term>
<term>Hemoglobins (chemistry)</term>
<term>Hemoglobins (metabolism)</term>
<term>Hydrogen Bonding (MeSH)</term>
<term>Nitric Oxide (chemistry)</term>
<term>Nitric Oxide (metabolism)</term>
<term>Oxygen (chemistry)</term>
<term>Oxygen (metabolism)</term>
<term>Spectrum Analysis, Raman (MeSH)</term>
<term>Structure-Activity Relationship (MeSH)</term>
<term>Truncated Hemoglobins (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Acides aminés (composition chimique)</term>
<term>Acides aminés (métabolisme)</term>
<term>Analyse spectrale Raman (MeSH)</term>
<term>Campylobacter jejuni (composition chimique)</term>
<term>Campylobacter jejuni (métabolisme)</term>
<term>Catalyse (MeSH)</term>
<term>Hémoglobines (composition chimique)</term>
<term>Hémoglobines (métabolisme)</term>
<term>Hémoglobines tronquées (MeSH)</term>
<term>Liaison hydrogène (MeSH)</term>
<term>Microbiologie alimentaire (MeSH)</term>
<term>Monoxyde d'azote (composition chimique)</term>
<term>Monoxyde d'azote (métabolisme)</term>
<term>Oxygène (composition chimique)</term>
<term>Oxygène (métabolisme)</term>
<term>Protéines bactériennes (MeSH)</term>
<term>Relation structure-activité (MeSH)</term>
<term>Sites de fixation (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Amino Acids</term>
<term>Hemoglobins</term>
<term>Nitric Oxide</term>
<term>Oxygen</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Amino Acids</term>
<term>Hemoglobins</term>
<term>Nitric Oxide</term>
<term>Oxygen</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Bacterial Proteins</term>
<term>Truncated Hemoglobins</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Campylobacter jejuni</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Acides aminés</term>
<term>Campylobacter jejuni</term>
<term>Hémoglobines</term>
<term>Monoxyde d'azote</term>
<term>Oxygène</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Campylobacter jejuni</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acides aminés</term>
<term>Campylobacter jejuni</term>
<term>Hémoglobines</term>
<term>Monoxyde d'azote</term>
<term>Oxygène</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term>
<term>Catalysis</term>
<term>Food Microbiology</term>
<term>Hydrogen Bonding</term>
<term>Spectrum Analysis, Raman</term>
<term>Structure-Activity Relationship</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Analyse spectrale Raman</term>
<term>Catalyse</term>
<term>Hémoglobines tronquées</term>
<term>Liaison hydrogène</term>
<term>Microbiologie alimentaire</term>
<term>Protéines bactériennes</term>
<term>Relation structure-activité</term>
<term>Sites de fixation</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Campylobacter jejuni contains two globins, a truncated hemoglobin, Ctb, and a single domain hemoglobin, Cgb. The physiological function of Ctb remains unclear, whereas Cgb has been linked to NO detoxification. With resonance Raman scattering, the iron-histidine stretching mode of Cgb was identified at 251 cm(-1). This frequency is unusually high, suggesting an imidazolate character of the proximal histidine as a result of the H-bonding network linking the catalytic triad involving the F8His, H23Glu, and G5Tyr residues. In the CO-complex, two conformers were identified with the nuC-O/nuFe-CO at 529/1914 cm(-1) and 492/1963 cm(-1). The former is assigned to a "closed" conformation, in which the heme-bound CO is stabilized by the H-bond(s) donated from the B10Tyr-E7Gln residues, whereas the latter is assigned to an "open" conformer, in which the H-bonding interaction is absent. The presence of the two alternative conformations demonstrates the plasticity of the protein matrix. In the O2-complex, the iron-O2 stretching frequency was identified at 554 cm(-1), which is unusually low, indicating that the heme-bound O2 is stabilized by strong H-bond(s) donated by the B10Tyr-E7Gln residues. This scenario is consistent with its low O2 off-rate (0.87 s(-1)). Taken together the data suggest that the NO-detoxifying activity of Cgb is facilitated by the imidazolate character of the proximal F8His and the distal positive polar environment provided by the B10Tyr-E7Gln. They may offer electronic "push" and "pull," respectively, for the O-O bond cleavage reaction required for the isomerization of the presumed peroxynitrite intermediate to the product, nitrate.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17606611</PMID>
<DateCompleted><Year>2007</Year>
<Month>10</Month>
<Day>29</Day>
</DateCompleted>
<DateRevised><Year>2017</Year>
<Month>09</Month>
<Day>22</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN>
<JournalIssue CitedMedium="Print"><Volume>282</Volume>
<Issue>35</Issue>
<PubDate><Year>2007</Year>
<Month>Aug</Month>
<Day>31</Day>
</PubDate>
</JournalIssue>
<Title>The Journal of biological chemistry</Title>
<ISOAbbreviation>J Biol Chem</ISOAbbreviation>
</Journal>
<ArticleTitle>Structural and functional properties of a single domain hemoglobin from the food-borne pathogen Campylobactor jejuni.</ArticleTitle>
<Pagination><MedlinePgn>25917-28</MedlinePgn>
</Pagination>
<Abstract><AbstractText>Campylobacter jejuni contains two globins, a truncated hemoglobin, Ctb, and a single domain hemoglobin, Cgb. The physiological function of Ctb remains unclear, whereas Cgb has been linked to NO detoxification. With resonance Raman scattering, the iron-histidine stretching mode of Cgb was identified at 251 cm(-1). This frequency is unusually high, suggesting an imidazolate character of the proximal histidine as a result of the H-bonding network linking the catalytic triad involving the F8His, H23Glu, and G5Tyr residues. In the CO-complex, two conformers were identified with the nuC-O/nuFe-CO at 529/1914 cm(-1) and 492/1963 cm(-1). The former is assigned to a "closed" conformation, in which the heme-bound CO is stabilized by the H-bond(s) donated from the B10Tyr-E7Gln residues, whereas the latter is assigned to an "open" conformer, in which the H-bonding interaction is absent. The presence of the two alternative conformations demonstrates the plasticity of the protein matrix. In the O2-complex, the iron-O2 stretching frequency was identified at 554 cm(-1), which is unusually low, indicating that the heme-bound O2 is stabilized by strong H-bond(s) donated by the B10Tyr-E7Gln residues. This scenario is consistent with its low O2 off-rate (0.87 s(-1)). Taken together the data suggest that the NO-detoxifying activity of Cgb is facilitated by the imidazolate character of the proximal F8His and the distal positive polar environment provided by the B10Tyr-E7Gln. They may offer electronic "push" and "pull," respectively, for the O-O bond cleavage reaction required for the isomerization of the presumed peroxynitrite intermediate to the product, nitrate.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lu</LastName>
<ForeName>Changyuan</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Mukai</LastName>
<ForeName>Masahiro</ForeName>
<Initials>M</Initials>
</Author>
<Author ValidYN="Y"><LastName>Lin</LastName>
<ForeName>Yu</ForeName>
<Initials>Y</Initials>
</Author>
<Author ValidYN="Y"><LastName>Wu</LastName>
<ForeName>Guanghui</ForeName>
<Initials>G</Initials>
</Author>
<Author ValidYN="Y"><LastName>Poole</LastName>
<ForeName>Robert K</ForeName>
<Initials>RK</Initials>
</Author>
<Author ValidYN="Y"><LastName>Yeh</LastName>
<ForeName>Syun-Ru</ForeName>
<Initials>SR</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>BB/E010504/1</GrantID>
<Agency>Biotechnology and Biological Sciences Research Council</Agency>
<Country>United Kingdom</Country>
</Grant>
<Grant><GrantID>HL65465</GrantID>
<Acronym>HL</Acronym>
<Agency>NHLBI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
</GrantList>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2007</Year>
<Month>07</Month>
<Day>02</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>J Biol Chem</MedlineTA>
<NlmUniqueID>2985121R</NlmUniqueID>
<ISSNLinking>0021-9258</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000596">Amino Acids</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C489659">Cgb protein, Campylobacter jejuni</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D006454">Hemoglobins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D054793">Truncated Hemoglobins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>31C4KY9ESH</RegistryNumber>
<NameOfSubstance UI="D009569">Nitric Oxide</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>S88TT14065</RegistryNumber>
<NameOfSubstance UI="D010100">Oxygen</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000596" MajorTopicYN="N">Amino Acids</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016123" MajorTopicYN="N">Campylobacter jejuni</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005516" MajorTopicYN="N">Food Microbiology</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006454" MajorTopicYN="N">Hemoglobins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006860" MajorTopicYN="N">Hydrogen Bonding</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009569" MajorTopicYN="N">Nitric Oxide</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010100" MajorTopicYN="N">Oxygen</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013059" MajorTopicYN="N">Spectrum Analysis, Raman</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013329" MajorTopicYN="N">Structure-Activity Relationship</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D054793" MajorTopicYN="N">Truncated Hemoglobins</DescriptorName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2007</Year>
<Month>7</Month>
<Day>4</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2007</Year>
<Month>10</Month>
<Day>30</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2007</Year>
<Month>7</Month>
<Day>4</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">17606611</ArticleId>
<ArticleId IdType="pii">M704415200</ArticleId>
<ArticleId IdType="doi">10.1074/jbc.M704415200</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>États-Unis</li>
</country>
</list>
<tree><noCountry><name sortKey="Lin, Yu" sort="Lin, Yu" uniqKey="Lin Y" first="Yu" last="Lin">Yu Lin</name>
<name sortKey="Mukai, Masahiro" sort="Mukai, Masahiro" uniqKey="Mukai M" first="Masahiro" last="Mukai">Masahiro Mukai</name>
<name sortKey="Poole, Robert K" sort="Poole, Robert K" uniqKey="Poole R" first="Robert K" last="Poole">Robert K. Poole</name>
<name sortKey="Wu, Guanghui" sort="Wu, Guanghui" uniqKey="Wu G" first="Guanghui" last="Wu">Guanghui Wu</name>
<name sortKey="Yeh, Syun Ru" sort="Yeh, Syun Ru" uniqKey="Yeh S" first="Syun-Ru" last="Yeh">Syun-Ru Yeh</name>
</noCountry>
<country name="États-Unis"><noRegion><name sortKey="Lu, Changyuan" sort="Lu, Changyuan" uniqKey="Lu C" first="Changyuan" last="Lu">Changyuan Lu</name>
</noRegion>
</country>
</tree>
</affiliations>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Bois/explor/DetoxFungiV1/Data/Main/Exploration

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002205 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 002205 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Bois
   |area=    DetoxFungiV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     pubmed:17606611
   |texte=   Structural and functional properties of a single domain hemoglobin from the food-borne pathogen Campylobactor jejuni.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i   -Sk "pubmed:17606611" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd   \
       | NlmPubMed2Wicri -a DetoxFungiV1

This area was generated with Dilib version V0.6.38.
Data generation: Fri Nov 20 16:09:04 2020. Site generation: Fri Nov 20 16:15:24 2020

	Serveur d'exploration sur la détoxication des champignons
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration sur la détoxication des champignons

Structural and functional properties of a single domain hemoglobin from the food-borne pathogen Campylobactor jejuni.

Structural and functional properties of a single domain hemoglobin from the food-borne pathogen Campylobactor jejuni.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki