Determinants of the relative reduction potentials of type-1 copper sites in proteins.
Identifieur interne : 004291 ( Main/Exploration ); précédent : 004290; suivant : 004292Determinants of the relative reduction potentials of type-1 copper sites in proteins.
Auteurs : Hui Li [États-Unis] ; Simon P. Webb ; Joseph Ivanic ; Jan H. JensenSource :
- Journal of the American Chemical Society [ 0002-7863 ] ; 2004.
Descripteurs français
- KwdFr :
- Azurine (analogues et dérivés), Azurine (composition chimique), Cuivre (composition chimique), Cuivre (métabolisme), Cystéine (composition chimique), Céruloplasmine (composition chimique), Humains (MeSH), Laccase (composition chimique), Liaison hydrogène (MeSH), Ligands (MeSH), Méthionine (composition chimique), Oxydoréduction (MeSH), Plastocyanine (composition chimique), Protéines (composition chimique), Sites de fixation (MeSH), Théorie quantique (MeSH).
- MESH :
- analogues et dérivés : Azurine.
- composition chimique : Azurine, Cuivre, Cystéine, Céruloplasmine, Laccase, Méthionine, Plastocyanine, Protéines.
- métabolisme : Cuivre.
- Humains, Liaison hydrogène, Ligands, Oxydoréduction, Sites de fixation, Théorie quantique.
English descriptors
- KwdEn :
- Azurin (analogs & derivatives), Azurin (chemistry), Binding Sites (MeSH), Ceruloplasmin (chemistry), Copper (chemistry), Copper (metabolism), Cysteine (chemistry), Humans (MeSH), Hydrogen Bonding (MeSH), Laccase (chemistry), Ligands (MeSH), Methionine (chemistry), Oxidation-Reduction (MeSH), Plastocyanin (chemistry), Proteins (chemistry), Quantum Theory (MeSH).
- MESH :
- chemical , analogs & derivatives : Azurin.
- chemical , chemistry : Azurin, Ceruloplasmin, Copper, Cysteine, Laccase, Methionine, Plastocyanin, Proteins.
- chemical , metabolism : Copper.
- Binding Sites, Humans, Hydrogen Bonding, Ligands, Oxidation-Reduction, Quantum Theory.
Abstract
The relative Cu(2+)/Cu(+) reduction potentials of six type-1 copper sites (cucumber stellacyanin, P. aeruginosa azurin, poplar plastocyanin, C. cinereus laccase, T. ferrooxidans rusticyanin, and human ceruloplasmin), which lie in a reduction potential range from 260 mV to over 1000 mV, have been studied by quantum mechanical calculations. The range and relative orderings of the reduction potentials are reproduced very well compared to experimental values. The study suggests that the main structural determinants of the relative reduction potentials of the blue copper sites are located within 6 A of the Cu atoms. Further analysis suggests that the reduction potential differences of type-1 copper sites are caused by axial ligand interactions, hydrogen bonding to the S(Cys), and protein constraint on the inner sphere ligand orientations. The low reduction potential of cucumber stellacyanin is due mainly to a glutamine ligand at the axial position, rather than a methionine or a hydrophobic residue as in the other proteins. A stronger interaction with a backbone carbonyl group is a prime contributor to the lower reduction potential of P. aeruginosa azurin as compared to poplar plastocyanin, whereas the reverse is true for C. cinereus laccase and T. ferrooxidans rusticyanin. The lack of an axial methonine ligand also contributes significantly to the increased reduction potentials of C. cinereus laccase and human ceruloplasmin. However, in the case of C. cinereus laccase, this increase is attenuated by the presence of only one amide NH hydrogen bond to the S(Cys) rather than two in the other proteins. In human ceruloplasmin the reduction potential is further increased by the structural distortion of the equatorial ligand orientation.
DOI: 10.1021/ja049345y
PubMed: 15212551
Affiliations:
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Webb</name></author><author><name sortKey="Ivanic, Joseph" sort="Ivanic, Joseph" uniqKey="Ivanic J" first="Joseph" last="Ivanic">Joseph Ivanic</name></author><author><name sortKey="Jensen, Jan H" sort="Jensen, Jan H" uniqKey="Jensen J" first="Jan H" last="Jensen">Jan H. 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Jensen</name></author></analytic><series><title level="j">Journal of the American Chemical Society</title><idno type="ISSN">0002-7863</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Azurin (analogs & derivatives)</term><term>Azurin (chemistry)</term><term>Binding Sites (MeSH)</term><term>Ceruloplasmin (chemistry)</term><term>Copper (chemistry)</term><term>Copper (metabolism)</term><term>Cysteine (chemistry)</term><term>Humans (MeSH)</term><term>Hydrogen Bonding (MeSH)</term><term>Laccase (chemistry)</term><term>Ligands (MeSH)</term><term>Methionine (chemistry)</term><term>Oxidation-Reduction (MeSH)</term><term>Plastocyanin (chemistry)</term><term>Proteins (chemistry)</term><term>Quantum Theory (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Azurine (analogues et dérivés)</term><term>Azurine (composition chimique)</term><term>Cuivre (composition chimique)</term><term>Cuivre (métabolisme)</term><term>Cystéine (composition chimique)</term><term>Céruloplasmine (composition chimique)</term><term>Humains (MeSH)</term><term>Laccase (composition chimique)</term><term>Liaison hydrogène (MeSH)</term><term>Ligands (MeSH)</term><term>Méthionine (composition chimique)</term><term>Oxydoréduction (MeSH)</term><term>Plastocyanine (composition chimique)</term><term>Protéines (composition chimique)</term><term>Sites de fixation (MeSH)</term><term>Théorie quantique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Azurin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Azurin</term><term>Ceruloplasmin</term><term>Copper</term><term>Cysteine</term><term>Laccase</term><term>Methionine</term><term>Plastocyanin</term><term>Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Copper</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Azurine</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Azurine</term><term>Cuivre</term><term>Cystéine</term><term>Céruloplasmine</term><term>Laccase</term><term>Méthionine</term><term>Plastocyanine</term><term>Protéines</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cuivre</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Humans</term><term>Hydrogen Bonding</term><term>Ligands</term><term>Oxidation-Reduction</term><term>Quantum Theory</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Humains</term><term>Liaison hydrogène</term><term>Ligands</term><term>Oxydoréduction</term><term>Sites de fixation</term><term>Théorie quantique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The relative Cu(2+)/Cu(+) reduction potentials of six type-1 copper sites (cucumber stellacyanin, P. aeruginosa azurin, poplar plastocyanin, C. cinereus laccase, T. ferrooxidans rusticyanin, and human ceruloplasmin), which lie in a reduction potential range from 260 mV to over 1000 mV, have been studied by quantum mechanical calculations. The range and relative orderings of the reduction potentials are reproduced very well compared to experimental values. The study suggests that the main structural determinants of the relative reduction potentials of the blue copper sites are located within 6 A of the Cu atoms. Further analysis suggests that the reduction potential differences of type-1 copper sites are caused by axial ligand interactions, hydrogen bonding to the S(Cys), and protein constraint on the inner sphere ligand orientations. The low reduction potential of cucumber stellacyanin is due mainly to a glutamine ligand at the axial position, rather than a methionine or a hydrophobic residue as in the other proteins. A stronger interaction with a backbone carbonyl group is a prime contributor to the lower reduction potential of P. aeruginosa azurin as compared to poplar plastocyanin, whereas the reverse is true for C. cinereus laccase and T. ferrooxidans rusticyanin. The lack of an axial methonine ligand also contributes significantly to the increased reduction potentials of C. cinereus laccase and human ceruloplasmin. However, in the case of C. cinereus laccase, this increase is attenuated by the presence of only one amide NH hydrogen bond to the S(Cys) rather than two in the other proteins. In human ceruloplasmin the reduction potential is further increased by the structural distortion of the equatorial ligand orientation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15212551</PMID><DateCompleted><Year>2004</Year><Month>09</Month><Day>07</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0002-7863</ISSN><JournalIssue CitedMedium="Print"><Volume>126</Volume><Issue>25</Issue><PubDate><Year>2004</Year><Month>Jun</Month><Day>30</Day></PubDate></JournalIssue><Title>Journal of the American Chemical Society</Title><ISOAbbreviation>J Am Chem Soc</ISOAbbreviation></Journal><ArticleTitle>Determinants of the relative reduction potentials of type-1 copper sites in proteins.</ArticleTitle><Pagination><MedlinePgn>8010-9</MedlinePgn></Pagination><Abstract><AbstractText>The relative Cu(2+)/Cu(+) reduction potentials of six type-1 copper sites (cucumber stellacyanin, P. aeruginosa azurin, poplar plastocyanin, C. cinereus laccase, T. ferrooxidans rusticyanin, and human ceruloplasmin), which lie in a reduction potential range from 260 mV to over 1000 mV, have been studied by quantum mechanical calculations. The range and relative orderings of the reduction potentials are reproduced very well compared to experimental values. The study suggests that the main structural determinants of the relative reduction potentials of the blue copper sites are located within 6 A of the Cu atoms. Further analysis suggests that the reduction potential differences of type-1 copper sites are caused by axial ligand interactions, hydrogen bonding to the S(Cys), and protein constraint on the inner sphere ligand orientations. The low reduction potential of cucumber stellacyanin is due mainly to a glutamine ligand at the axial position, rather than a methionine or a hydrophobic residue as in the other proteins. A stronger interaction with a backbone carbonyl group is a prime contributor to the lower reduction potential of P. aeruginosa azurin as compared to poplar plastocyanin, whereas the reverse is true for C. cinereus laccase and T. ferrooxidans rusticyanin. The lack of an axial methonine ligand also contributes significantly to the increased reduction potentials of C. cinereus laccase and human ceruloplasmin. However, in the case of C. cinereus laccase, this increase is attenuated by the presence of only one amide NH hydrogen bond to the S(Cys) rather than two in the other proteins. In human ceruloplasmin the reduction potential is further increased by the structural distortion of the equatorial ligand orientation.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Hui</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Department of Chemistry, The University of Iowa, Iowa City, Iowa 52242, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Webb</LastName><ForeName>Simon P</ForeName><Initials>SP</Initials></Author><Author ValidYN="Y"><LastName>Ivanic</LastName><ForeName>Joseph</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Jensen</LastName><ForeName>Jan H</ForeName><Initials>JH</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>N01-CO-12400</GrantID><Acronym>CO</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Am Chem Soc</MedlineTA><NlmUniqueID>7503056</NlmUniqueID><ISSNLinking>0002-7863</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008024">Ligands</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C012543">rusticyanin</NameOfSubstance></Chemical><Chemical><RegistryNumber>12284-43-4</RegistryNumber><NameOfSubstance UI="D001400">Azurin</NameOfSubstance></Chemical><Chemical><RegistryNumber>789U1901C5</RegistryNumber><NameOfSubstance UI="D003300">Copper</NameOfSubstance></Chemical><Chemical><RegistryNumber>9014-09-9</RegistryNumber><NameOfSubstance UI="D010970">Plastocyanin</NameOfSubstance></Chemical><Chemical><RegistryNumber>AE28F7PNPL</RegistryNumber><NameOfSubstance UI="D008715">Methionine</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.10.3.2</RegistryNumber><NameOfSubstance UI="D042845">Laccase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.16.3.1</RegistryNumber><NameOfSubstance UI="D002570">Ceruloplasmin</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001400" MajorTopicYN="N">Azurin</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002570" MajorTopicYN="N">Ceruloplasmin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><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="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006860" MajorTopicYN="N">Hydrogen Bonding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D042845" MajorTopicYN="N">Laccase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008024" MajorTopicYN="N">Ligands</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008715" MajorTopicYN="N">Methionine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010970" MajorTopicYN="N">Plastocyanin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011789" MajorTopicYN="N">Quantum Theory</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2004</Year><Month>6</Month><Day>24</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2004</Year><Month>9</Month><Day>8</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2004</Year><Month>6</Month><Day>24</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15212551</ArticleId><ArticleId IdType="doi">10.1021/ja049345y</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Iowa</li></region><settlement><li>Iowa City</li></settlement><orgName><li>Université de l'Iowa</li></orgName></list><tree><noCountry><name sortKey="Ivanic, Joseph" sort="Ivanic, Joseph" uniqKey="Ivanic J" first="Joseph" last="Ivanic">Joseph Ivanic</name><name sortKey="Jensen, Jan H" sort="Jensen, Jan H" uniqKey="Jensen J" first="Jan H" last="Jensen">Jan H. Jensen</name><name sortKey="Webb, Simon P" sort="Webb, Simon P" uniqKey="Webb S" first="Simon P" last="Webb">Simon P. Webb</name></noCountry><country name="États-Unis"><region name="Iowa"><name sortKey="Li, Hui" sort="Li, Hui" uniqKey="Li H" first="Hui" last="Li">Hui Li</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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