UV Raman monitoring of histidine protonation and H-(2)H exchange in plastocyanin.
Identifieur interne : 004526 ( Main/Exploration ); précédent : 004525; suivant : 004527UV Raman monitoring of histidine protonation and H-(2)H exchange in plastocyanin.
Auteurs : Qiang Wu [États-Unis] ; Fangbiao Li ; Weixun Wang ; Michael H. Hecht ; Thomas G. SpiroSource :
- Journal of inorganic biochemistry [ 0162-0134 ] ; 2002.
Descripteurs français
- KwdFr :
- Analyse spectrale Raman (MeSH), Concentration en ions d'hydrogène (MeSH), Conformation des protéines (MeSH), Cuivre (composition chimique), Cuivre (métabolisme), Histidine (composition chimique), Histidine (métabolisme), Plastocyanine (composition chimique), Plastocyanine (métabolisme), Protons (MeSH).
- MESH :
- composition chimique : Cuivre, Histidine, Plastocyanine.
- métabolisme : Cuivre, Histidine, Plastocyanine.
- Analyse spectrale Raman, Concentration en ions d'hydrogène, Conformation des protéines, Protons.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Copper, Histidine, Plastocyanin.
- chemical , metabolism : Copper, Histidine, Plastocyanin.
- Hydrogen-Ion Concentration, Protein Conformation, Protons, Spectrum Analysis, Raman.
Abstract
UV resonance Raman bands of Cu-bound and protonated histidine residues have been detected in (2)H(2)O solutions of poplar plastocyanin. For the Cu(II) protein, slow NH-(2)H exchange of the His37 ligand was monitored via the growth of bands at 1389 and 1344 cm(-1) when Pcy was exchanged into (2)H(2)O, or via their diminution when the protein was exchanged back into H(2)O; the rate constant is 7 x 10(-4)/s at pH (p(2)H) 7.4 at room temperature. The slow exchange is attributed to imidazole H-bonding to a backbone carbonyl. Nearby bands at 1397 and 1354 cm(-1), appear and disappear within the mixing time, and are assigned to the solvent-exposed His87 ligand. The approximately 10 cm(-1) differences between His37 and His87 are attributed to the effect of H-bonding on the imidazole ring modes. The UVRR spectra of the Cu(I) protein in (2)H(2)O reveal a 1408 cm(-1) band, characteristic of NH-(2)H-exchanged histidinium, which grows in as the p(2)H is lowered. Its intensity follows a titration curve with pK(a)=4.6. This protonation is assigned to the His87 residue, whose bond to the Cu(I) is known from crystallography to be broken at low pH. As the 1408 cm(-1) band grows, a band at 1345 cm(-1) diminishes, while another, at 1337 cm(-1) stays constant. These are assigned to modes of bound His87 and His37, respectively, shifted down 7-9 cm(-1) from their Cu(II) positions.
DOI: 10.1016/s0162-0134(01)00354-3
PubMed: 11897354
Affiliations:
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Hecht</name></author><author><name sortKey="Spiro, Thomas G" sort="Spiro, Thomas G" uniqKey="Spiro T" first="Thomas G" last="Spiro">Thomas G. Spiro</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2002">2002</date><idno type="RBID">pubmed:11897354</idno><idno type="pmid">11897354</idno><idno type="doi">10.1016/s0162-0134(01)00354-3</idno><idno type="wicri:Area/Main/Corpus">004673</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">004673</idno><idno type="wicri:Area/Main/Curation">004673</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">004673</idno><idno type="wicri:Area/Main/Exploration">004673</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">UV Raman monitoring of histidine protonation and H-(2)H exchange in plastocyanin.</title><author><name sortKey="Wu, Qiang" sort="Wu, Qiang" uniqKey="Wu Q" first="Qiang" last="Wu">Qiang Wu</name><affiliation wicri:level="4"><nlm:affiliation>Department of Chemistry, Princeton University, Princeton, NJ 08544, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry, Princeton University, Princeton, NJ 08544</wicri:regionArea><placeName><region type="state">New Jersey</region><settlement type="city">Princeton (New Jersey)</settlement></placeName><orgName type="university">Université de Princeton</orgName></affiliation></author><author><name sortKey="Li, Fangbiao" sort="Li, Fangbiao" uniqKey="Li F" first="Fangbiao" last="Li">Fangbiao Li</name></author><author><name sortKey="Wang, Weixun" sort="Wang, Weixun" uniqKey="Wang W" first="Weixun" last="Wang">Weixun Wang</name></author><author><name sortKey="Hecht, Michael H" sort="Hecht, Michael H" uniqKey="Hecht M" first="Michael H" last="Hecht">Michael H. Hecht</name></author><author><name sortKey="Spiro, Thomas G" sort="Spiro, Thomas G" uniqKey="Spiro T" first="Thomas G" last="Spiro">Thomas G. Spiro</name></author></analytic><series><title level="j">Journal of inorganic biochemistry</title><idno type="ISSN">0162-0134</idno><imprint><date when="2002" type="published">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Copper (chemistry)</term><term>Copper (metabolism)</term><term>Histidine (chemistry)</term><term>Histidine (metabolism)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Plastocyanin (chemistry)</term><term>Plastocyanin (metabolism)</term><term>Protein Conformation (MeSH)</term><term>Protons (MeSH)</term><term>Spectrum Analysis, Raman (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Analyse spectrale Raman (MeSH)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Cuivre (composition chimique)</term><term>Cuivre (métabolisme)</term><term>Histidine (composition chimique)</term><term>Histidine (métabolisme)</term><term>Plastocyanine (composition chimique)</term><term>Plastocyanine (métabolisme)</term><term>Protons (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Copper</term><term>Histidine</term><term>Plastocyanin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Copper</term><term>Histidine</term><term>Plastocyanin</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cuivre</term><term>Histidine</term><term>Plastocyanine</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cuivre</term><term>Histidine</term><term>Plastocyanine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Hydrogen-Ion Concentration</term><term>Protein Conformation</term><term>Protons</term><term>Spectrum Analysis, Raman</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse spectrale Raman</term><term>Concentration en ions d'hydrogène</term><term>Conformation des protéines</term><term>Protons</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">UV resonance Raman bands of Cu-bound and protonated histidine residues have been detected in (2)H(2)O solutions of poplar plastocyanin. For the Cu(II) protein, slow NH-(2)H exchange of the His37 ligand was monitored via the growth of bands at 1389 and 1344 cm(-1) when Pcy was exchanged into (2)H(2)O, or via their diminution when the protein was exchanged back into H(2)O; the rate constant is 7 x 10(-4)/s at pH (p(2)H) 7.4 at room temperature. The slow exchange is attributed to imidazole H-bonding to a backbone carbonyl. Nearby bands at 1397 and 1354 cm(-1), appear and disappear within the mixing time, and are assigned to the solvent-exposed His87 ligand. The approximately 10 cm(-1) differences between His37 and His87 are attributed to the effect of H-bonding on the imidazole ring modes. The UVRR spectra of the Cu(I) protein in (2)H(2)O reveal a 1408 cm(-1) band, characteristic of NH-(2)H-exchanged histidinium, which grows in as the p(2)H is lowered. Its intensity follows a titration curve with pK(a)=4.6. This protonation is assigned to the His87 residue, whose bond to the Cu(I) is known from crystallography to be broken at low pH. As the 1408 cm(-1) band grows, a band at 1345 cm(-1) diminishes, while another, at 1337 cm(-1) stays constant. These are assigned to modes of bound His87 and His37, respectively, shifted down 7-9 cm(-1) from their Cu(II) positions.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11897354</PMID><DateCompleted><Year>2002</Year><Month>06</Month><Day>12</Day></DateCompleted><DateRevised><Year>2019</Year><Month>09</Month><Day>10</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0162-0134</ISSN><JournalIssue CitedMedium="Print"><Volume>88</Volume><Issue>3-4</Issue><PubDate><Year>2002</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Journal of inorganic biochemistry</Title><ISOAbbreviation>J Inorg Biochem</ISOAbbreviation></Journal><ArticleTitle>UV Raman monitoring of histidine protonation and H-(2)H exchange in plastocyanin.</ArticleTitle><Pagination><MedlinePgn>381-7</MedlinePgn></Pagination><Abstract><AbstractText>UV resonance Raman bands of Cu-bound and protonated histidine residues have been detected in (2)H(2)O solutions of poplar plastocyanin. For the Cu(II) protein, slow NH-(2)H exchange of the His37 ligand was monitored via the growth of bands at 1389 and 1344 cm(-1) when Pcy was exchanged into (2)H(2)O, or via their diminution when the protein was exchanged back into H(2)O; the rate constant is 7 x 10(-4)/s at pH (p(2)H) 7.4 at room temperature. The slow exchange is attributed to imidazole H-bonding to a backbone carbonyl. Nearby bands at 1397 and 1354 cm(-1), appear and disappear within the mixing time, and are assigned to the solvent-exposed His87 ligand. The approximately 10 cm(-1) differences between His37 and His87 are attributed to the effect of H-bonding on the imidazole ring modes. The UVRR spectra of the Cu(I) protein in (2)H(2)O reveal a 1408 cm(-1) band, characteristic of NH-(2)H-exchanged histidinium, which grows in as the p(2)H is lowered. Its intensity follows a titration curve with pK(a)=4.6. This protonation is assigned to the His87 residue, whose bond to the Cu(I) is known from crystallography to be broken at low pH. As the 1408 cm(-1) band grows, a band at 1345 cm(-1) diminishes, while another, at 1337 cm(-1) stays constant. These are assigned to modes of bound His87 and His37, respectively, shifted down 7-9 cm(-1) from their Cu(II) positions.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wu</LastName><ForeName>Qiang</ForeName><Initials>Q</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Princeton University, Princeton, NJ 08544, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Fangbiao</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Weixun</ForeName><Initials>W</Initials></Author><Author ValidYN="Y"><LastName>Hecht</LastName><ForeName>Michael H</ForeName><Initials>MH</Initials></Author><Author ValidYN="Y"><LastName>Spiro</LastName><ForeName>Thomas G</ForeName><Initials>TG</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>GM 33576</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Inorg Biochem</MedlineTA><NlmUniqueID>7905788</NlmUniqueID><ISSNLinking>0162-0134</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011522">Protons</NameOfSubstance></Chemical><Chemical><RegistryNumber>4QD397987E</RegistryNumber><NameOfSubstance UI="D006639">Histidine</NameOfSubstance></Chemical><Chemical><RegistryNumber>789U1901C5</RegistryNumber><NameOfSubstance UI="D003300">Copper</NameOfSubstance></Chemical><Chemical><RegistryNumber>9014-09-9</RegistryNumber><NameOfSubstance UI="D010970">Plastocyanin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D003300" MajorTopicYN="N">Copper</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006639" MajorTopicYN="N">Histidine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010970" MajorTopicYN="N">Plastocyanin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011522" MajorTopicYN="N">Protons</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013059" MajorTopicYN="N">Spectrum Analysis, Raman</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>3</Month><Day>19</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2002</Year><Month>6</Month><Day>13</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2002</Year><Month>3</Month><Day>19</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11897354</ArticleId><ArticleId IdType="pii">S0162013401003543</ArticleId><ArticleId IdType="doi">10.1016/s0162-0134(01)00354-3</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>New Jersey</li></region><settlement><li>Princeton (New Jersey)</li></settlement><orgName><li>Université de Princeton</li></orgName></list><tree><noCountry><name sortKey="Hecht, Michael H" sort="Hecht, Michael H" uniqKey="Hecht M" first="Michael H" last="Hecht">Michael H. Hecht</name><name sortKey="Li, Fangbiao" sort="Li, Fangbiao" uniqKey="Li F" first="Fangbiao" last="Li">Fangbiao Li</name><name sortKey="Spiro, Thomas G" sort="Spiro, Thomas G" uniqKey="Spiro T" first="Thomas G" last="Spiro">Thomas G. Spiro</name><name sortKey="Wang, Weixun" sort="Wang, Weixun" uniqKey="Wang W" first="Weixun" last="Wang">Weixun Wang</name></noCountry><country name="États-Unis"><region name="New Jersey"><name sortKey="Wu, Qiang" sort="Wu, Qiang" uniqKey="Wu Q" first="Qiang" last="Wu">Qiang Wu</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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