Insights into copper coordination in the EcoRI-DNA complex by ESR spectroscopy.
Identifieur interne : 000D29 ( PubMed/Curation ); précédent : 000D28; suivant : 000D30Insights into copper coordination in the EcoRI-DNA complex by ESR spectroscopy.
Auteurs : Ming Ji [États-Unis] ; Likun Tan [États-Unis] ; Linda Jen-Jacobson [États-Unis] ; Sunil Saxena [États-Unis]Source :
- 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 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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<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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