The species and heme pocket properties of sturgeon hemoglobins upon interaction with N-dodecyl trimethylammonium bromide.
Identifieur interne : 000223 ( PubMed/Corpus ); précédent : 000222; suivant : 000224The species and heme pocket properties of sturgeon hemoglobins upon interaction with N-dodecyl trimethylammonium bromide.
Auteurs : Shohreh Ariaeenejad ; Ali A. Moosavi-Movahedi ; Kaveh Kavousi ; Mohammad Reza Dayer ; Jun Hong ; Reza Yousefi ; Nader Sheibani ; Mehran Habibi-RezaeiSource :
- Protein and peptide letters [ 1875-5305 ] ; 2014.
English descriptors
- KwdEn :
- Animals, Fish Proteins (chemistry), Fish Proteins (metabolism), Fishes, Heme (metabolism), Hemoglobins (chemistry), Hemoglobins (metabolism), Oxygen (metabolism), Protein Binding, Protein Conformation (drug effects), Quaternary Ammonium Compounds (metabolism), Quaternary Ammonium Compounds (pharmacology), Species Specificity.
- MESH :
- chemical , chemistry : Fish Proteins, Hemoglobins.
- chemical , metabolism : Fish Proteins, Heme, Hemoglobins, Oxygen, Quaternary Ammonium Compounds.
- drug effects : Protein Conformation.
- chemical , pharmacology : Quaternary Ammonium Compounds.
- Animals, Fishes, Protein Binding, Species Specificity.
Abstract
The variations in fish hemoglobin (Hb) structures play a vital role in their respiratory performance under various environmental conditions and are impacted by their physiological properties. The major hemoglobins from two species of sturgeon were studied upon interaction with n-dodecyl trimethyl ammonium bromide (DTAB) using the UV-vis absorption, circular dichroism (CD), fluorescence spectroscopy, and oxygen affinity measurement methods as well as chemometric analysis. The UV-Vis absorption spectra between 500 and 650 nm was used to identify each species of hemoglobin, and to show that the concentration of oxyHb and metHb decreases, while that of deoxyHb increases upon interaction with DTAB. Both reduced oxyHb and oxidized hemichrome of the two Hbs were studied to obtain information about the DTAB efects on their structural features. The circular dichroism (CD) was utilized to obtain secondary structure and compactness for Hb upon interaction with DTAB. Binding of DTAB molecules induced the unfolding of Hb, and was accompanied with exposure of the heme pocket facilitating its oxidation. The differences between unfolding processes for the two Acipenser species were indicated by fluorescence spectroscopy. The chemometric analysis of Hbs was investigated upon interaction with DTAB under titration, using fluorescence spectra allowing determination of the number of components and mole fractions of the oxidized Hb. Our data showed that Acipenser persicus Hb had a more hyperchromic character, more surface area, more loosely folded structure, and therefore, exposed region of heme group compared with Acipenser stellatus oxyHb. In addition, with increasing DTAB the transition of Acipenser stellatus oxyHb to the state of hemichrome occurred at a slower speed than Acipenser persicus oxyHb, and finally more oxygen affinity and compactness. Our results suggest that these differences aroused from the inherent differences between the heme groups which fulfil a potentially important physiological role in these fish.
PubMed: 24000823
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The species and heme pocket properties of sturgeon hemoglobins upon interaction with N-dodecyl trimethylammonium bromide.</title><author><name sortKey="Ariaeenejad, Shohreh" sort="Ariaeenejad, Shohreh" uniqKey="Ariaeenejad S" first="Shohreh" last="Ariaeenejad">Shohreh Ariaeenejad</name></author><author><name sortKey="Moosavi Movahedi, Ali A" sort="Moosavi Movahedi, Ali A" uniqKey="Moosavi Movahedi A" first="Ali A" last="Moosavi-Movahedi">Ali A. Moosavi-Movahedi</name></author><author><name sortKey="Kavousi, Kaveh" sort="Kavousi, Kaveh" uniqKey="Kavousi K" first="Kaveh" last="Kavousi">Kaveh Kavousi</name></author><author><name sortKey="Dayer, Mohammad Reza" sort="Dayer, Mohammad Reza" uniqKey="Dayer M" first="Mohammad Reza" last="Dayer">Mohammad Reza Dayer</name></author><author><name sortKey="Hong, Jun" sort="Hong, Jun" uniqKey="Hong J" first="Jun" last="Hong">Jun Hong</name></author><author><name sortKey="Yousefi, Reza" sort="Yousefi, Reza" uniqKey="Yousefi R" first="Reza" last="Yousefi">Reza Yousefi</name></author><author><name sortKey="Sheibani, Nader" sort="Sheibani, Nader" uniqKey="Sheibani N" first="Nader" last="Sheibani">Nader Sheibani</name></author><author><name sortKey="Habibi Rezaei, Mehran" sort="Habibi Rezaei, Mehran" uniqKey="Habibi Rezaei M" first="Mehran" last="Habibi-Rezaei">Mehran Habibi-Rezaei</name><affiliation><nlm:affiliation>Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran. moosavi@ut.ac.ir.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:24000823</idno><idno type="pmid">24000823</idno><idno type="wicri:Area/PubMed/Corpus">000223</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000223</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The species and heme pocket properties of sturgeon hemoglobins upon interaction with N-dodecyl trimethylammonium bromide.</title><author><name sortKey="Ariaeenejad, Shohreh" sort="Ariaeenejad, Shohreh" uniqKey="Ariaeenejad S" first="Shohreh" last="Ariaeenejad">Shohreh Ariaeenejad</name></author><author><name sortKey="Moosavi Movahedi, Ali A" sort="Moosavi Movahedi, Ali A" uniqKey="Moosavi Movahedi A" first="Ali A" last="Moosavi-Movahedi">Ali A. Moosavi-Movahedi</name></author><author><name sortKey="Kavousi, Kaveh" sort="Kavousi, Kaveh" uniqKey="Kavousi K" first="Kaveh" last="Kavousi">Kaveh Kavousi</name></author><author><name sortKey="Dayer, Mohammad Reza" sort="Dayer, Mohammad Reza" uniqKey="Dayer M" first="Mohammad Reza" last="Dayer">Mohammad Reza Dayer</name></author><author><name sortKey="Hong, Jun" sort="Hong, Jun" uniqKey="Hong J" first="Jun" last="Hong">Jun Hong</name></author><author><name sortKey="Yousefi, Reza" sort="Yousefi, Reza" uniqKey="Yousefi R" first="Reza" last="Yousefi">Reza Yousefi</name></author><author><name sortKey="Sheibani, Nader" sort="Sheibani, Nader" uniqKey="Sheibani N" first="Nader" last="Sheibani">Nader Sheibani</name></author><author><name sortKey="Habibi Rezaei, Mehran" sort="Habibi Rezaei, Mehran" uniqKey="Habibi Rezaei M" first="Mehran" last="Habibi-Rezaei">Mehran Habibi-Rezaei</name><affiliation><nlm:affiliation>Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran. moosavi@ut.ac.ir.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Protein and peptide letters</title><idno type="eISSN">1875-5305</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Fish Proteins (chemistry)</term><term>Fish Proteins (metabolism)</term><term>Fishes</term><term>Heme (metabolism)</term><term>Hemoglobins (chemistry)</term><term>Hemoglobins (metabolism)</term><term>Oxygen (metabolism)</term><term>Protein Binding</term><term>Protein Conformation (drug effects)</term><term>Quaternary Ammonium Compounds (metabolism)</term><term>Quaternary Ammonium Compounds (pharmacology)</term><term>Species Specificity</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Fish Proteins</term><term>Hemoglobins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Fish Proteins</term><term>Heme</term><term>Hemoglobins</term><term>Oxygen</term><term>Quaternary Ammonium Compounds</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Protein Conformation</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Quaternary Ammonium Compounds</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Fishes</term><term>Protein Binding</term><term>Species Specificity</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The variations in fish hemoglobin (Hb) structures play a vital role in their respiratory performance under various environmental conditions and are impacted by their physiological properties. The major hemoglobins from two species of sturgeon were studied upon interaction with n-dodecyl trimethyl ammonium bromide (DTAB) using the UV-vis absorption, circular dichroism (CD), fluorescence spectroscopy, and oxygen affinity measurement methods as well as chemometric analysis. The UV-Vis absorption spectra between 500 and 650 nm was used to identify each species of hemoglobin, and to show that the concentration of oxyHb and metHb decreases, while that of deoxyHb increases upon interaction with DTAB. Both reduced oxyHb and oxidized hemichrome of the two Hbs were studied to obtain information about the DTAB efects on their structural features. The circular dichroism (CD) was utilized to obtain secondary structure and compactness for Hb upon interaction with DTAB. Binding of DTAB molecules induced the unfolding of Hb, and was accompanied with exposure of the heme pocket facilitating its oxidation. The differences between unfolding processes for the two Acipenser species were indicated by fluorescence spectroscopy. The chemometric analysis of Hbs was investigated upon interaction with DTAB under titration, using fluorescence spectra allowing determination of the number of components and mole fractions of the oxidized Hb. Our data showed that Acipenser persicus Hb had a more hyperchromic character, more surface area, more loosely folded structure, and therefore, exposed region of heme group compared with Acipenser stellatus oxyHb. In addition, with increasing DTAB the transition of Acipenser stellatus oxyHb to the state of hemichrome occurred at a slower speed than Acipenser persicus oxyHb, and finally more oxygen affinity and compactness. Our results suggest that these differences aroused from the inherent differences between the heme groups which fulfil a potentially important physiological role in these fish.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24000823</PMID><DateCreated><Year>2013</Year><Month>12</Month><Day>27</Day></DateCreated><DateCompleted><Year>2014</Year><Month>09</Month><Day>29</Day></DateCompleted><DateRevised><Year>2016</Year><Month>12</Month><Day>29</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1875-5305</ISSN><JournalIssue CitedMedium="Internet"><Volume>21</Volume><Issue>2</Issue><PubDate><Year>2014</Year></PubDate></JournalIssue><Title>Protein and peptide letters</Title><ISOAbbreviation>Protein Pept. Lett.</ISOAbbreviation></Journal><ArticleTitle>The species and heme pocket properties of sturgeon hemoglobins upon interaction with N-dodecyl trimethylammonium bromide.</ArticleTitle><Pagination><MedlinePgn>171-8</MedlinePgn></Pagination><Abstract><AbstractText>The variations in fish hemoglobin (Hb) structures play a vital role in their respiratory performance under various environmental conditions and are impacted by their physiological properties. The major hemoglobins from two species of sturgeon were studied upon interaction with n-dodecyl trimethyl ammonium bromide (DTAB) using the UV-vis absorption, circular dichroism (CD), fluorescence spectroscopy, and oxygen affinity measurement methods as well as chemometric analysis. The UV-Vis absorption spectra between 500 and 650 nm was used to identify each species of hemoglobin, and to show that the concentration of oxyHb and metHb decreases, while that of deoxyHb increases upon interaction with DTAB. Both reduced oxyHb and oxidized hemichrome of the two Hbs were studied to obtain information about the DTAB efects on their structural features. The circular dichroism (CD) was utilized to obtain secondary structure and compactness for Hb upon interaction with DTAB. Binding of DTAB molecules induced the unfolding of Hb, and was accompanied with exposure of the heme pocket facilitating its oxidation. The differences between unfolding processes for the two Acipenser species were indicated by fluorescence spectroscopy. The chemometric analysis of Hbs was investigated upon interaction with DTAB under titration, using fluorescence spectra allowing determination of the number of components and mole fractions of the oxidized Hb. Our data showed that Acipenser persicus Hb had a more hyperchromic character, more surface area, more loosely folded structure, and therefore, exposed region of heme group compared with Acipenser stellatus oxyHb. In addition, with increasing DTAB the transition of Acipenser stellatus oxyHb to the state of hemichrome occurred at a slower speed than Acipenser persicus oxyHb, and finally more oxygen affinity and compactness. Our results suggest that these differences aroused from the inherent differences between the heme groups which fulfil a potentially important physiological role in these fish.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ariaeenejad</LastName><ForeName>Shohreh</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Moosavi-Movahedi</LastName><ForeName>Ali A</ForeName><Initials>AA</Initials></Author><Author ValidYN="Y"><LastName>Kavousi</LastName><ForeName>Kaveh</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Dayer</LastName><ForeName>Mohammad Reza</ForeName><Initials>MR</Initials></Author><Author ValidYN="Y"><LastName>Hong</LastName><ForeName>Jun</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Yousefi</LastName><ForeName>Reza</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Sheibani</LastName><ForeName>Nader</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Habibi-Rezaei</LastName><ForeName>Mehran</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran. moosavi@ut.ac.ir.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>RC4 EY021357</GrantID><Acronym>EY</Acronym><Agency>NEI NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Protein Pept Lett</MedlineTA><NlmUniqueID>9441434</NlmUniqueID><ISSNLinking>0929-8665</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029941">Fish Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006454">Hemoglobins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000644">Quaternary Ammonium Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>15053-09-5</RegistryNumber><NameOfSubstance UI="C013912">decyltrimethylammonium</NameOfSubstance></Chemical><Chemical><RegistryNumber>42VZT0U6YR</RegistryNumber><NameOfSubstance UI="D006418">Heme</NameOfSubstance></Chemical><Chemical><RegistryNumber>S88TT14065</RegistryNumber><NameOfSubstance UI="D010100">Oxygen</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D029941" MajorTopicYN="N">Fish Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005399" MajorTopicYN="Y">Fishes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006418" MajorTopicYN="N">Heme</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006454" MajorTopicYN="N">Hemoglobins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010100" MajorTopicYN="N">Oxygen</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000644" MajorTopicYN="N">Quaternary Ammonium Compounds</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013045" MajorTopicYN="N">Species Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>07</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2013</Year><Month>08</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2013</Year><Month>08</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>9</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>9</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>9</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24000823</ArticleId><ArticleId IdType="pii">PPL-EPUB-55746</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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