Structural comparison of the poplar plastocyanin isoforms PCa and PCb sheds new light on the role of the copper site geometry in interactions with redox partners in oxygenic photosynthesis.
Identifieur interne : 002906 ( Main/Exploration ); précédent : 002905; suivant : 002907Structural comparison of the poplar plastocyanin isoforms PCa and PCb sheds new light on the role of the copper site geometry in interactions with redox partners in oxygenic photosynthesis.
Auteurs : Galina S. Kachalova [Russie] ; Alexandra C. Shosheva ; Gleb P. Bourenkov ; Anthony A. Donchev ; Mitko I. Dimitrov ; Hans D. BartunikSource :
- Journal of inorganic biochemistry [ 1873-3344 ] ; 2012.
Descripteurs français
- KwdFr :
- Complexe protéique du photosystème I (composition chimique), Complexe protéique du photosystème I (métabolisme), Concentration en ions d'hydrogène (MeSH), Cuivre (composition chimique), Cuivre (métabolisme), Cytochromes f (composition chimique), Cytochromes f (métabolisme), Isoformes de protéines (composition chimique), Isoformes de protéines (métabolisme), Oxydoréduction (MeSH), Photosynthèse (physiologie), Plastocyanine (composition chimique), Plastocyanine (métabolisme), Populus (composition chimique), Populus (métabolisme).
- MESH :
- composition chimique : Complexe protéique du photosystème I, Cuivre, Cytochromes f, Isoformes de protéines, Plastocyanine, Populus.
- métabolisme : Complexe protéique du photosystème I, Cuivre, Cytochromes f, Isoformes de protéines, Plastocyanine, Populus.
- physiologie : Photosynthèse.
- Concentration en ions d'hydrogène, Oxydoréduction.
English descriptors
- KwdEn :
- Copper (chemistry), Copper (metabolism), Cytochromes f (chemistry), Cytochromes f (metabolism), Hydrogen-Ion Concentration (MeSH), Oxidation-Reduction (MeSH), Photosynthesis (physiology), Photosystem I Protein Complex (chemistry), Photosystem I Protein Complex (metabolism), Plastocyanin (chemistry), Plastocyanin (metabolism), Populus (chemistry), Populus (metabolism), Protein Isoforms (chemistry), Protein Isoforms (metabolism).
- MESH :
- chemical , chemistry : Copper, Cytochromes f, Photosystem I Protein Complex, Plastocyanin, Protein Isoforms.
- chemical , metabolism : Copper, Cytochromes f, Photosystem I Protein Complex, Plastocyanin, Protein Isoforms.
- chemistry : Populus.
- metabolism : Populus.
- physiology : Photosynthesis.
- Hydrogen-Ion Concentration, Oxidation-Reduction.
Abstract
Plastocyanin (PC) from poplar leaves is present in two isoforms, PCa and PCb, which differ in sequence by amino acid replacements at locations remote from the copper center and simultaneously act in the photosynthetic electron-transport chain. We describe ultra-high resolution structures of PCa and high-resolution structures of PCb, both under oxidizing and reducing conditions at pH 4, 6 and 8. The docking on cytochrome f and photosystem I, respectively, has been modeled for both isoforms. PCa and PCb exhibit closely similar overall and active-site structures, except for a difference in the relative orientation of the acidic patches. The isoforms exhibit substantial differences in the dependence of the reduced (Cu(I)) geometry on pH. In PCa, the decrease in pH causes a gradual dissociation of His87 from Cu(I) at low pH, probably adopting a neutral tautomeric state. In PCb, the histidine remains covalently bound to Cu(I) and may adopt a doubly protonated state at low pH. The fact that both isoforms have similar although not identical functions in photosynthetic electron flows suggests that the His87 imidazole does not play a crucial role for the pathway of electron transport from cytochrome f to oxidized PC.
DOI: 10.1016/j.jinorgbio.2012.07.015
PubMed: 22883960
Affiliations:
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Donchev</name></author><author><name sortKey="Dimitrov, Mitko I" sort="Dimitrov, Mitko I" uniqKey="Dimitrov M" first="Mitko I" last="Dimitrov">Mitko I. Dimitrov</name></author><author><name sortKey="Bartunik, Hans D" sort="Bartunik, Hans D" uniqKey="Bartunik H" first="Hans D" last="Bartunik">Hans D. 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We describe ultra-high resolution structures of PCa and high-resolution structures of PCb, both under oxidizing and reducing conditions at pH 4, 6 and 8. The docking on cytochrome f and photosystem I, respectively, has been modeled for both isoforms. PCa and PCb exhibit closely similar overall and active-site structures, except for a difference in the relative orientation of the acidic patches. The isoforms exhibit substantial differences in the dependence of the reduced (Cu(I)) geometry on pH. In PCa, the decrease in pH causes a gradual dissociation of His87 from Cu(I) at low pH, probably adopting a neutral tautomeric state. In PCb, the histidine remains covalently bound to Cu(I) and may adopt a doubly protonated state at low pH. The fact that both isoforms have similar although not identical functions in photosynthetic electron flows suggests that the His87 imidazole does not play a crucial role for the pathway of electron transport from cytochrome f to oxidized PC.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22883960</PMID><DateCompleted><Year>2013</Year><Month>02</Month><Day>14</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-3344</ISSN><JournalIssue CitedMedium="Internet"><Volume>115</Volume><PubDate><Year>2012</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Journal of inorganic biochemistry</Title><ISOAbbreviation>J Inorg Biochem</ISOAbbreviation></Journal><ArticleTitle>Structural comparison of the poplar plastocyanin isoforms PCa and PCb sheds new light on the role of the copper site geometry in interactions with redox partners in oxygenic photosynthesis.</ArticleTitle><Pagination><MedlinePgn>174-81</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.jinorgbio.2012.07.015</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0162-0134(12)00233-4</ELocationID><Abstract><AbstractText>Plastocyanin (PC) from poplar leaves is present in two isoforms, PCa and PCb, which differ in sequence by amino acid replacements at locations remote from the copper center and simultaneously act in the photosynthetic electron-transport chain. We describe ultra-high resolution structures of PCa and high-resolution structures of PCb, both under oxidizing and reducing conditions at pH 4, 6 and 8. The docking on cytochrome f and photosystem I, respectively, has been modeled for both isoforms. PCa and PCb exhibit closely similar overall and active-site structures, except for a difference in the relative orientation of the acidic patches. The isoforms exhibit substantial differences in the dependence of the reduced (Cu(I)) geometry on pH. In PCa, the decrease in pH causes a gradual dissociation of His87 from Cu(I) at low pH, probably adopting a neutral tautomeric state. In PCb, the histidine remains covalently bound to Cu(I) and may adopt a doubly protonated state at low pH. The fact that both isoforms have similar although not identical functions in photosynthetic electron flows suggests that the His87 imidazole does not play a crucial role for the pathway of electron transport from cytochrome f to oxidized PC.</AbstractText><CopyrightInformation>Copyright © 2012 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kachalova</LastName><ForeName>Galina S</ForeName><Initials>GS</Initials><AffiliationInfo><Affiliation>A.N.Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr., Moscow 119071, Russia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shosheva</LastName><ForeName>Alexandra C</ForeName><Initials>AC</Initials></Author><Author ValidYN="Y"><LastName>Bourenkov</LastName><ForeName>Gleb P</ForeName><Initials>GP</Initials></Author><Author ValidYN="Y"><LastName>Donchev</LastName><ForeName>Anthony A</ForeName><Initials>AA</Initials></Author><Author ValidYN="Y"><LastName>Dimitrov</LastName><ForeName>Mitko I</ForeName><Initials>MI</Initials></Author><Author ValidYN="Y"><LastName>Bartunik</LastName><ForeName>Hans D</ForeName><Initials>HD</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2012</Year><Month>07</Month><Day>20</Day></ArticleDate></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="D045331">Photosystem I Protein Complex</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020033">Protein Isoforms</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>9035-46-5</RegistryNumber><NameOfSubstance UI="D045348">Cytochromes f</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D003300" MajorTopicYN="Y">Copper</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045348" MajorTopicYN="N">Cytochromes f</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010788" MajorTopicYN="N">Photosynthesis</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045331" MajorTopicYN="N">Photosystem I Protein Complex</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010970" MajorTopicYN="Y">Plastocyanin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="Y">Populus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020033" MajorTopicYN="N">Protein Isoforms</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>03</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2012</Year><Month>07</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2012</Year><Month>07</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2012</Year><Month>8</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2012</Year><Month>8</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>2</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">22883960</ArticleId><ArticleId IdType="pii">S0162-0134(12)00233-4</ArticleId><ArticleId IdType="doi">10.1016/j.jinorgbio.2012.07.015</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Russie</li></country><region><li>District fédéral central</li></region><settlement><li>Moscou</li></settlement></list><tree><noCountry><name sortKey="Bartunik, Hans D" sort="Bartunik, Hans D" uniqKey="Bartunik H" first="Hans D" last="Bartunik">Hans D. Bartunik</name><name sortKey="Bourenkov, Gleb P" sort="Bourenkov, Gleb P" uniqKey="Bourenkov G" first="Gleb P" last="Bourenkov">Gleb P. Bourenkov</name><name sortKey="Dimitrov, Mitko I" sort="Dimitrov, Mitko I" uniqKey="Dimitrov M" first="Mitko I" last="Dimitrov">Mitko I. Dimitrov</name><name sortKey="Donchev, Anthony A" sort="Donchev, Anthony A" uniqKey="Donchev A" first="Anthony A" last="Donchev">Anthony A. Donchev</name><name sortKey="Shosheva, Alexandra C" sort="Shosheva, Alexandra C" uniqKey="Shosheva A" first="Alexandra C" last="Shosheva">Alexandra C. Shosheva</name></noCountry><country name="Russie"><region name="District fédéral central"><name sortKey="Kachalova, Galina S" sort="Kachalova, Galina S" uniqKey="Kachalova G" first="Galina S" last="Kachalova">Galina S. Kachalova</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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