Insights into copper coordination in the EcoRI–DNA complex by ESR spectroscopy
Identifieur interne : 001A06 ( Pmc/Corpus ); précédent : 001A05; suivant : 001A07Insights into copper coordination in the EcoRI–DNA complex by ESR spectroscopy
Auteurs : Ming Ji ; Likun Tan ; Linda Jen-Jacobson ; Sunil SaxenaSource :
- Molecular physics [ 0026-8976 ] ; 2014.
Abstract
The EcoRI restriction endonuclease requires one divalent metal ion in each of two symmetrical and identical catalytic sites to catalyse double-strand DNA cleavage. Recently, we showed that Cu2+ binds outside the catalytic sites to a pair of new sites at H114 in each sub-unit, and inhibits Mg2+ -catalysed DNA cleavage. In order to provide more detailed structural information on this new metal ion binding site, we performed W-band (~94 GHz) and X-band (~9.5 GHz) electron spin resonance spectroscopic measurements on the EcoRI–DNA–(Cu2+ )2 complex. Cu2+ binding results in two distinct components with different
Url:
DOI: 10.1080/00268976.2014.934313
PubMed: 25750461
PubMed Central: 4350447
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Insights into copper coordination in the EcoRI–DNA complex by ESR spectroscopy</title><author><name sortKey="Ji, Ming" sort="Ji, Ming" uniqKey="Ji M" first="Ming" last="Ji">Ming Ji</name><affiliation><nlm:aff id="A1">Department of Chemistry, University of Pittsburgh, Pittsburgh, PA, USA</nlm:aff></affiliation></author><author><name sortKey="Tan, Likun" sort="Tan, Likun" uniqKey="Tan L" first="Likun" last="Tan">Likun Tan</name><affiliation><nlm:aff id="A2">Division of Engineering and Applied Science, California Institute of Technology, Pasadena, CA, USA</nlm:aff></affiliation></author><author><name sortKey="Jen Jacobson, Linda" sort="Jen Jacobson, Linda" uniqKey="Jen Jacobson L" first="Linda" last="Jen-Jacobson">Linda Jen-Jacobson</name><affiliation><nlm:aff id="A3">Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA, USA</nlm:aff></affiliation></author><author><name sortKey="Saxena, Sunil" sort="Saxena, Sunil" uniqKey="Saxena S" first="Sunil" last="Saxena">Sunil Saxena</name><affiliation><nlm:aff id="A1">Department of Chemistry, University of Pittsburgh, Pittsburgh, PA, USA</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">25750461</idno><idno type="pmc">4350447</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4350447</idno><idno type="RBID">PMC:4350447</idno><idno type="doi">10.1080/00268976.2014.934313</idno><date when="2014">2014</date><idno type="wicri:Area/Pmc/Corpus">001A06</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">001A06</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Insights into copper coordination in the EcoRI–DNA complex by ESR spectroscopy</title><author><name sortKey="Ji, Ming" sort="Ji, Ming" uniqKey="Ji M" first="Ming" last="Ji">Ming Ji</name><affiliation><nlm:aff id="A1">Department of Chemistry, University of Pittsburgh, Pittsburgh, PA, USA</nlm:aff></affiliation></author><author><name sortKey="Tan, Likun" sort="Tan, Likun" uniqKey="Tan L" first="Likun" last="Tan">Likun Tan</name><affiliation><nlm:aff id="A2">Division of Engineering and Applied Science, California Institute of Technology, Pasadena, CA, USA</nlm:aff></affiliation></author><author><name sortKey="Jen Jacobson, Linda" sort="Jen Jacobson, Linda" uniqKey="Jen Jacobson L" first="Linda" last="Jen-Jacobson">Linda Jen-Jacobson</name><affiliation><nlm:aff id="A3">Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA, USA</nlm:aff></affiliation></author><author><name sortKey="Saxena, Sunil" sort="Saxena, Sunil" uniqKey="Saxena S" first="Sunil" last="Saxena">Sunil Saxena</name><affiliation><nlm:aff id="A1">Department of Chemistry, University of Pittsburgh, Pittsburgh, PA, USA</nlm:aff></affiliation></author></analytic><series><title level="j">Molecular physics</title><idno type="ISSN">0026-8976</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p id="P1">The EcoRI restriction endonuclease requires one divalent metal ion in each of two symmetrical and identical catalytic sites to catalyse double-strand DNA cleavage. Recently, we showed that Cu<sup>2+</sup> binds outside the catalytic sites to a pair of new sites at H114 in each sub-unit, and inhibits Mg<sup>2+</sup> -catalysed DNA cleavage. In order to provide more detailed structural information on this new metal ion binding site, we performed W-band (~94 GHz) and X-band (~9.5 GHz) electron spin resonance spectroscopic measurements on the EcoRI–DNA–(Cu<sup>2+</sup> )<sub>2</sub> complex. Cu<sup>2+</sup> binding results in two distinct components with different <italic>g</italic><sub>zz</sub> and <italic>A</italic><sub>zz</sub> values. X-band electron spin echo envelope modulation results indicate that both components arise from a Cu<sup>2+</sup> coordinated to histidine. This observation is further confirmed by the hyperfine sub-level correlation results. W-band electron nuclear double resonance spectra provide evidence for equatorial coordination of water molecules to the Cu<sup>2+</sup> ions.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<pmc-dir>properties manuscript</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-journal-id">9876329</journal-id><journal-id journal-id-type="pubmed-jr-id">22852</journal-id><journal-id journal-id-type="nlm-ta">Mol Phys</journal-id><journal-id journal-id-type="iso-abbrev">Mol Phys</journal-id><journal-title-group><journal-title>Molecular physics</journal-title></journal-title-group><issn pub-type="ppub">0026-8976</issn></journal-meta><article-meta><article-id pub-id-type="pmid">25750461</article-id><article-id pub-id-type="pmc">4350447</article-id><article-id pub-id-type="doi">10.1080/00268976.2014.934313</article-id><article-id pub-id-type="manuscript">NIHMS667213</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Insights into copper coordination in the EcoRI–DNA complex by ESR spectroscopy</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Ji</surname><given-names>Ming</given-names></name><xref ref-type="aff" rid="A1">a</xref></contrib><contrib contrib-type="author"><name><surname>Tan</surname><given-names>Likun</given-names></name><xref ref-type="aff" rid="A2">b</xref></contrib><contrib contrib-type="author"><name><surname>Jen-Jacobson</surname><given-names>Linda</given-names></name><xref ref-type="aff" rid="A3">c</xref></contrib><contrib contrib-type="author"><name><surname>Saxena</surname><given-names>Sunil</given-names></name><xref ref-type="aff" rid="A1">a</xref><xref ref-type="corresp" rid="CR1">*</xref></contrib></contrib-group><aff id="A1"><label>a</label>Department of Chemistry, University of Pittsburgh, Pittsburgh, PA, USA</aff><aff id="A2"><label>b</label>Division of Engineering and Applied Science, California Institute of Technology, Pasadena, CA, USA</aff><aff id="A3"><label>c</label>Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA, USA</aff><author-notes><corresp id="CR1"><label>*</label>Corresponding author. <email>sksaxena@pitt.edu</email></corresp></author-notes><pub-date pub-type="nihms-submitted"><day>26</day><month>2</month><year>2015</year></pub-date><pub-date pub-type="epub"><day>10</day><month>7</month><year>2014</year></pub-date><pub-date pub-type="ppub"><day>1</day><month>12</month><year>2014</year></pub-date><pub-date pub-type="pmc-release"><day>05</day><month>3</month><year>2015</year></pub-date><volume>112</volume><issue>24</issue><fpage>3173</fpage><lpage>3182</lpage><pmc-comment>elocation-id from pubmed: 10.1080/00268976.2014.934313</pmc-comment>
<permissions><copyright-statement>© 2014 Taylor & Francis</copyright-statement><copyright-year>2014</copyright-year><license><license-p>This article may be used for research, teaching, and private study purposes. Any substantial or systematic reproduction, redistribution, reselling, loan, sub-licensing, systematic supply, or distribution in any form to anyone is expressly forbidden. Terms & Conditions of access and use can be found at <ext-link ext-link-type="uri" xlink:href="http://www.tandfonline.com/page/terms-and-conditions">http://www.tandfonline.com/page/terms-and-conditions</ext-link></license-p></license></permissions><abstract><p id="P1">The EcoRI restriction endonuclease requires one divalent metal ion in each of two symmetrical and identical catalytic sites to catalyse double-strand DNA cleavage. Recently, we showed that Cu<sup>2+</sup> binds outside the catalytic sites to a pair of new sites at H114 in each sub-unit, and inhibits Mg<sup>2+</sup> -catalysed DNA cleavage. In order to provide more detailed structural information on this new metal ion binding site, we performed W-band (~94 GHz) and X-band (~9.5 GHz) electron spin resonance spectroscopic measurements on the EcoRI–DNA–(Cu<sup>2+</sup> )<sub>2</sub> complex. Cu<sup>2+</sup> binding results in two distinct components with different <italic>g</italic><sub>zz</sub> and <italic>A</italic><sub>zz</sub> values. X-band electron spin echo envelope modulation results indicate that both components arise from a Cu<sup>2+</sup> coordinated to histidine. This observation is further confirmed by the hyperfine sub-level correlation results. W-band electron nuclear double resonance spectra provide evidence for equatorial coordination of water molecules to the Cu<sup>2+</sup> ions.</p></abstract><kwd-group><kwd>W-band ENDOR</kwd><kwd>ESEEM</kwd><kwd>metal ion coordination</kwd><kwd>Cu<sup>2+</sup> inhibition</kwd><kwd>restriction endonuclease</kwd></kwd-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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