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Insights into copper coordination in the EcoRI-DNA complex by ESR spectroscopy.

Identifieur interne : 000D29 ( PubMed/Corpus ); précédent : 000D28; suivant : 000D30

Insights into copper coordination in the EcoRI-DNA complex by ESR spectroscopy.

Auteurs : Ming Ji ; Likun Tan ; Linda Jen-Jacobson ; Sunil Saxena

Source :

Molecular physics [ 0026-8976 ] ; 2014.

RBID : pubmed:25750461

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 Cu(2+) binds outside the catalytic sites to a pair of new sites at H114 in each sub-unit, and inhibits Mg(2+) -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(2+) )2 complex. Cu(2+) binding results in two distinct components with different gzz and Azz values. X-band electron spin echo envelope modulation results indicate that both components arise from a Cu(2+) 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(2+) ions.

DOI: 10.1080/00268976.2014.934313
PubMed: 25750461

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<author><name sortKey="Ji, Ming" sort="Ji, Ming" uniqKey="Ji M" first="Ming" last="Ji">Ming Ji</name>
<affiliation><nlm:affiliation>Department of Chemistry, University of Pittsburgh, Pittsburgh, PA, USA.</nlm:affiliation>
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<author><name sortKey="Tan, Likun" sort="Tan, Likun" uniqKey="Tan L" first="Likun" last="Tan">Likun Tan</name>
<affiliation><nlm:affiliation>Division of Engineering and Applied Science, California Institute of Technology, Pasadena, CA, USA.</nlm:affiliation>
</affiliation>
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<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:affiliation>Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA, USA.</nlm:affiliation>
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<author><name sortKey="Saxena, Sunil" sort="Saxena, Sunil" uniqKey="Saxena S" first="Sunil" last="Saxena">Sunil Saxena</name>
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<front><div type="abstract" xml:lang="en">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(2+) binds outside the catalytic sites to a pair of new sites at H114 in each sub-unit, and inhibits Mg(2+) -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(2+) )2 complex. Cu(2+) binding results in two distinct components with different gzz and Azz values. X-band electron spin echo envelope modulation results indicate that both components arise from a Cu(2+) 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(2+) ions.</div>
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<Abstract><AbstractText>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(2+) binds outside the catalytic sites to a pair of new sites at H114 in each sub-unit, and inhibits Mg(2+) -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(2+) )2 complex. Cu(2+) binding results in two distinct components with different gzz and Azz values. X-band electron spin echo envelope modulation results indicate that both components arise from a Cu(2+) 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(2+) ions.</AbstractText>
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Insights into copper coordination in the EcoRI-DNA complex by ESR spectroscopy.

Insights into copper coordination in the EcoRI-DNA complex by ESR spectroscopy.

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