The transient complex of poplar plastocyanin with cytochrome f: effects of ionic strength and pH.
Identifieur interne : 004070 ( Main/Corpus ); précédent : 004069; suivant : 004071The transient complex of poplar plastocyanin with cytochrome f: effects of ionic strength and pH.
Auteurs : Christian Lange ; Tobias Cornvik ; Irene Díaz-Moreno ; Marcellus UbbinkSource :
- Biochimica et biophysica acta [ 0006-3002 ]
English descriptors
- KwdEn :
- Brassica napus (MeSH), Cytochromes f (chemistry), Cytochromes f (metabolism), Hydrogen-Ion Concentration (MeSH), Models, Molecular (MeSH), Nuclear Magnetic Resonance, Biomolecular (MeSH), Osmolar Concentration (MeSH), Plant Proteins (chemistry), Plant Proteins (metabolism), Plastocyanin (chemistry), Plastocyanin (metabolism), Protein Binding (MeSH), Protein Conformation (MeSH), Time Factors (MeSH), Trees (MeSH).
- MESH :
- chemical , chemistry : Cytochromes f, Plant Proteins, Plastocyanin.
- chemical , metabolism : Cytochromes f, Plant Proteins, Plastocyanin.
- Brassica napus, Hydrogen-Ion Concentration, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Osmolar Concentration, Protein Binding, Protein Conformation, Time Factors, Trees.
Abstract
The orientation of poplar plastocyanin in the complex with turnip cytochrome f has been determined by rigid-body calculations using restraints from paramagnetic NMR measurements. The results show that poplar plastocyanin interacts with cytochrome f with the hydrophobic patch of plastocyanin close to the heme region on cytochrome f and via electrostatic interactions between the charged patches on both proteins. Plastocyanin is tilted relative to the orientation reported for spinach plastocyanin, resulting in a longer distance between iron and copper (13.9 A). With increasing ionic strength, from 0.01 to 0.11 M, all observed chemical-shift changes decrease uniformly, supporting the idea that electrostatic forces contribute to complex formation. There is no indication for a rearrangement of the transient complex in this ionic strength range, contrary to what had been proposed earlier on the basis of kinetic data. By decreasing the pH from pH 7.7 to pH 5.5, the complex is destabilized. This may be attributed to the protonation of the conserved acidic patches or the copper ligand His87 in poplar plastocyanin, which are shown to have similar pK(a) values. The results are interpreted in a two-step model for complex formation.
DOI: 10.1016/j.bbabio.2004.12.002
PubMed: 15863096
Links to Exploration step
pubmed:15863096Le document en format XML
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Box 9502, 2300 RA Leiden, The Netherlands.</nlm:affiliation></affiliation></author><author><name sortKey="Cornvik, Tobias" sort="Cornvik, Tobias" uniqKey="Cornvik T" first="Tobias" last="Cornvik">Tobias Cornvik</name></author><author><name sortKey="Diaz Moreno, Irene" sort="Diaz Moreno, Irene" uniqKey="Diaz Moreno I" first="Irene" last="Díaz-Moreno">Irene Díaz-Moreno</name></author><author><name sortKey="Ubbink, Marcellus" sort="Ubbink, Marcellus" uniqKey="Ubbink M" first="Marcellus" last="Ubbink">Marcellus Ubbink</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2005">2005 Apr-May</date><idno type="RBID">pubmed:15863096</idno><idno type="pmid">15863096</idno><idno type="doi">10.1016/j.bbabio.2004.12.002</idno><idno type="wicri:Area/Main/Corpus">004070</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">004070</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The transient complex of poplar plastocyanin with cytochrome f: effects of ionic strength and pH.</title><author><name sortKey="Lange, Christian" sort="Lange, Christian" uniqKey="Lange C" first="Christian" last="Lange">Christian Lange</name><affiliation><nlm:affiliation>Leiden Institute of Chemistry, Leiden University, Gorlaeus Laboratories, P.O. Box 9502, 2300 RA Leiden, The Netherlands.</nlm:affiliation></affiliation></author><author><name sortKey="Cornvik, Tobias" sort="Cornvik, Tobias" uniqKey="Cornvik T" first="Tobias" last="Cornvik">Tobias Cornvik</name></author><author><name sortKey="Diaz Moreno, Irene" sort="Diaz Moreno, Irene" uniqKey="Diaz Moreno I" first="Irene" last="Díaz-Moreno">Irene Díaz-Moreno</name></author><author><name sortKey="Ubbink, Marcellus" sort="Ubbink, Marcellus" uniqKey="Ubbink M" first="Marcellus" last="Ubbink">Marcellus Ubbink</name></author></analytic><series><title level="j">Biochimica et biophysica acta</title><idno type="ISSN">0006-3002</idno></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Brassica napus (MeSH)</term><term>Cytochromes f (chemistry)</term><term>Cytochromes f (metabolism)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Nuclear Magnetic Resonance, Biomolecular (MeSH)</term><term>Osmolar Concentration (MeSH)</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (metabolism)</term><term>Plastocyanin (chemistry)</term><term>Plastocyanin (metabolism)</term><term>Protein Binding (MeSH)</term><term>Protein Conformation (MeSH)</term><term>Time Factors (MeSH)</term><term>Trees (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cytochromes f</term><term>Plant Proteins</term><term>Plastocyanin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cytochromes f</term><term>Plant Proteins</term><term>Plastocyanin</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Brassica napus</term><term>Hydrogen-Ion Concentration</term><term>Models, Molecular</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Osmolar Concentration</term><term>Protein Binding</term><term>Protein Conformation</term><term>Time Factors</term><term>Trees</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The orientation of poplar plastocyanin in the complex with turnip cytochrome f has been determined by rigid-body calculations using restraints from paramagnetic NMR measurements. The results show that poplar plastocyanin interacts with cytochrome f with the hydrophobic patch of plastocyanin close to the heme region on cytochrome f and via electrostatic interactions between the charged patches on both proteins. Plastocyanin is tilted relative to the orientation reported for spinach plastocyanin, resulting in a longer distance between iron and copper (13.9 A). With increasing ionic strength, from 0.01 to 0.11 M, all observed chemical-shift changes decrease uniformly, supporting the idea that electrostatic forces contribute to complex formation. There is no indication for a rearrangement of the transient complex in this ionic strength range, contrary to what had been proposed earlier on the basis of kinetic data. By decreasing the pH from pH 7.7 to pH 5.5, the complex is destabilized. This may be attributed to the protonation of the conserved acidic patches or the copper ligand His87 in poplar plastocyanin, which are shown to have similar pK(a) values. The results are interpreted in a two-step model for complex formation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15863096</PMID><DateCompleted><Year>2005</Year><Month>07</Month><Day>14</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>26</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1707</Volume><Issue>2-3</Issue><PubDate><MedlineDate>2005 Apr-May</MedlineDate></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim Biophys Acta</ISOAbbreviation></Journal><ArticleTitle>The transient complex of poplar plastocyanin with cytochrome f: effects of ionic strength and pH.</ArticleTitle><Pagination><MedlinePgn>179-88</MedlinePgn></Pagination><Abstract><AbstractText>The orientation of poplar plastocyanin in the complex with turnip cytochrome f has been determined by rigid-body calculations using restraints from paramagnetic NMR measurements. The results show that poplar plastocyanin interacts with cytochrome f with the hydrophobic patch of plastocyanin close to the heme region on cytochrome f and via electrostatic interactions between the charged patches on both proteins. Plastocyanin is tilted relative to the orientation reported for spinach plastocyanin, resulting in a longer distance between iron and copper (13.9 A). With increasing ionic strength, from 0.01 to 0.11 M, all observed chemical-shift changes decrease uniformly, supporting the idea that electrostatic forces contribute to complex formation. There is no indication for a rearrangement of the transient complex in this ionic strength range, contrary to what had been proposed earlier on the basis of kinetic data. By decreasing the pH from pH 7.7 to pH 5.5, the complex is destabilized. This may be attributed to the protonation of the conserved acidic patches or the copper ligand His87 in poplar plastocyanin, which are shown to have similar pK(a) values. The results are interpreted in a two-step model for complex formation.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lange</LastName><ForeName>Christian</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Leiden Institute of Chemistry, Leiden University, Gorlaeus Laboratories, P.O. Box 9502, 2300 RA Leiden, The Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cornvik</LastName><ForeName>Tobias</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Díaz-Moreno</LastName><ForeName>Irene</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Ubbink</LastName><ForeName>Marcellus</ForeName><Initials>M</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2004</Year><Month>12</Month><Day>29</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta</MedlineTA><NlmUniqueID>0217513</NlmUniqueID><ISSNLinking>0006-3002</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>9014-09-9</RegistryNumber><NameOfSubstance UI="D010970">Plastocyanin</NameOfSubstance></Chemical><Chemical><RegistryNumber>9035-46-5</RegistryNumber><NameOfSubstance UI="D045348">Cytochromes f</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D029688" MajorTopicYN="N">Brassica napus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045348" MajorTopicYN="N">Cytochromes f</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="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019906" MajorTopicYN="N">Nuclear Magnetic Resonance, Biomolecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009994" MajorTopicYN="N">Osmolar Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></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="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013997" MajorTopicYN="N">Time Factors</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014197" MajorTopicYN="N">Trees</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2004</Year><Month>08</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2004</Year><Month>11</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2004</Year><Month>12</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2005</Year><Month>5</Month><Day>3</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>7</Month><Day>15</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>5</Month><Day>3</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15863096</ArticleId><ArticleId IdType="pii">S0005-2728(04)00338-X</ArticleId><ArticleId IdType="doi">10.1016/j.bbabio.2004.12.002</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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