Low Temperature 65Cu NMR Spectroscopy of the Cu+ Site in Azurin
65Cu central-transition NMR spectroscopy of the blue copper protein azurin in the reduced Cu(I) state, conducted at 18.8 T and 10 K, gave a strongly second order quadrupole perturbed spectrum, which yielded a 65Cu quadrupole coupling constant of ±71.2 ± 1 MHz, corresponding to an electric field grad...
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| Veröffentlicht in: | Journal of the American Chemical Society 2009-10, Vol.131 (39), p.13992-13999 |
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| container_issue | 39 |
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| container_title | Journal of the American Chemical Society |
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| creator | Lipton, Andrew S Heck, Robert W de Jong, Wibe A Gao, Amy R Wu, Xiongjian Roehrich, Adrienne Harbison, Gerard S Ellis, Paul D |
| description | 65Cu central-transition NMR spectroscopy of the blue copper protein azurin in the reduced Cu(I) state, conducted at 18.8 T and 10 K, gave a strongly second order quadrupole perturbed spectrum, which yielded a 65Cu quadrupole coupling constant of ±71.2 ± 1 MHz, corresponding to an electric field gradient of ±1.49 atomic units at the copper site, and an asymmetry parameter of approximately 0.2. Quantum chemical calculations employing second order Møller−Plesset perturbation theory and large basis sets successfully reproduced these experimental results. Sensitivity and relaxation times were quite favorable, suggesting that NMR may be a useful probe of the electronic state of copper sites in proteins. |
| doi_str_mv | 10.1021/ja901308v |
| format | Article |
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Quantum chemical calculations employing second order Møller−Plesset perturbation theory and large basis sets successfully reproduced these experimental results. Sensitivity and relaxation times were quite favorable, suggesting that NMR may be a useful probe of the electronic state of copper sites in proteins.</description><identifier>ISSN: 0002-7863</identifier><identifier>EISSN: 1520-5126</identifier><identifier>DOI: 10.1021/ja901308v</identifier><identifier>PMID: 19746904</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Azurin - chemistry ; Catalytic Domain ; Cold Temperature ; Copper - chemistry ; Isotopes - chemistry ; Models, Chemical ; Nuclear Magnetic Resonance, Biomolecular ; Quantum Theory</subject><ispartof>Journal of the American Chemical Society, 2009-10, Vol.131 (39), p.13992-13999</ispartof><rights>Copyright © 2009 American Chemical Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/ja901308v$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/ja901308v$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>230,314,776,780,881,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19746904$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lipton, Andrew S</creatorcontrib><creatorcontrib>Heck, Robert W</creatorcontrib><creatorcontrib>de Jong, Wibe A</creatorcontrib><creatorcontrib>Gao, Amy R</creatorcontrib><creatorcontrib>Wu, Xiongjian</creatorcontrib><creatorcontrib>Roehrich, Adrienne</creatorcontrib><creatorcontrib>Harbison, Gerard S</creatorcontrib><creatorcontrib>Ellis, Paul D</creatorcontrib><title>Low Temperature 65Cu NMR Spectroscopy of the Cu+ Site in Azurin</title><title>Journal of the American Chemical Society</title><addtitle>J. Am. Chem. Soc</addtitle><description>65Cu central-transition NMR spectroscopy of the blue copper protein azurin in the reduced Cu(I) state, conducted at 18.8 T and 10 K, gave a strongly second order quadrupole perturbed spectrum, which yielded a 65Cu quadrupole coupling constant of ±71.2 ± 1 MHz, corresponding to an electric field gradient of ±1.49 atomic units at the copper site, and an asymmetry parameter of approximately 0.2. Quantum chemical calculations employing second order Møller−Plesset perturbation theory and large basis sets successfully reproduced these experimental results. Sensitivity and relaxation times were quite favorable, suggesting that NMR may be a useful probe of the electronic state of copper sites in proteins.</description><subject>Azurin - chemistry</subject><subject>Catalytic Domain</subject><subject>Cold Temperature</subject><subject>Copper - chemistry</subject><subject>Isotopes - chemistry</subject><subject>Models, Chemical</subject><subject>Nuclear Magnetic Resonance, Biomolecular</subject><subject>Quantum Theory</subject><issn>0002-7863</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkUtLw0AUhQdRbK0u_AMyG3Eh0Xkkd5KNUoIvqAq2rofJdKIpSSbOJJX66420Fl1dDvfjHO49CB1TckEJo5cLlRDKSbzcQUMaMRJElMEuGhJCWCBi4AN04P2ilyGL6T4a0ESEkJBwiK4n9hPPTNUYp9rOGQxR2uGnxxc8bYxunfXaNitsc9y-G5x253hatAYXNR5_da6oD9FerkpvjjZzhF5vb2bpfTB5vntIx5NAUREtgwRinmvCYwCgAFxkRMUs1wAJ0Axo2EtqeKa0yRMuBKNZNIc5F0miDdWcj9DV2rfpssrMtalbp0rZuKJSbiWtKuT_TV28yze7lEzEDID1BmcbA2c_OuNbWRVem7JUtbGdl4KHBELCwp48-Ru1zfh9Wg-crgGlvVzYztX95ZIS-VOG3JbBvwG7XHfL</recordid><startdate>20091007</startdate><enddate>20091007</enddate><creator>Lipton, Andrew S</creator><creator>Heck, Robert W</creator><creator>de Jong, Wibe A</creator><creator>Gao, Amy R</creator><creator>Wu, Xiongjian</creator><creator>Roehrich, Adrienne</creator><creator>Harbison, Gerard S</creator><creator>Ellis, Paul D</creator><general>American Chemical Society</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20091007</creationdate><title>Low Temperature 65Cu NMR Spectroscopy of the Cu+ Site in Azurin</title><author>Lipton, Andrew S ; Heck, Robert W ; de Jong, Wibe A ; Gao, Amy R ; Wu, Xiongjian ; Roehrich, Adrienne ; Harbison, Gerard S ; Ellis, Paul D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a175v-9683fc03866616637b0a82fc66961b6140a81e3bacef937721b5d6d3799ce1c33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Azurin - chemistry</topic><topic>Catalytic Domain</topic><topic>Cold Temperature</topic><topic>Copper - chemistry</topic><topic>Isotopes - chemistry</topic><topic>Models, Chemical</topic><topic>Nuclear Magnetic Resonance, Biomolecular</topic><topic>Quantum Theory</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lipton, Andrew S</creatorcontrib><creatorcontrib>Heck, Robert W</creatorcontrib><creatorcontrib>de Jong, Wibe A</creatorcontrib><creatorcontrib>Gao, Amy R</creatorcontrib><creatorcontrib>Wu, Xiongjian</creatorcontrib><creatorcontrib>Roehrich, Adrienne</creatorcontrib><creatorcontrib>Harbison, Gerard S</creatorcontrib><creatorcontrib>Ellis, Paul D</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lipton, Andrew S</au><au>Heck, Robert W</au><au>de Jong, Wibe A</au><au>Gao, Amy R</au><au>Wu, Xiongjian</au><au>Roehrich, Adrienne</au><au>Harbison, Gerard S</au><au>Ellis, Paul D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Low Temperature 65Cu NMR Spectroscopy of the Cu+ Site in Azurin</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>2009-10-07</date><risdate>2009</risdate><volume>131</volume><issue>39</issue><spage>13992</spage><epage>13999</epage><pages>13992-13999</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><abstract>65Cu central-transition NMR spectroscopy of the blue copper protein azurin in the reduced Cu(I) state, conducted at 18.8 T and 10 K, gave a strongly second order quadrupole perturbed spectrum, which yielded a 65Cu quadrupole coupling constant of ±71.2 ± 1 MHz, corresponding to an electric field gradient of ±1.49 atomic units at the copper site, and an asymmetry parameter of approximately 0.2. Quantum chemical calculations employing second order Møller−Plesset perturbation theory and large basis sets successfully reproduced these experimental results. Sensitivity and relaxation times were quite favorable, suggesting that NMR may be a useful probe of the electronic state of copper sites in proteins.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>19746904</pmid><doi>10.1021/ja901308v</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| source | ACS Publications; MEDLINE |
| subjects | Azurin - chemistry Catalytic Domain Cold Temperature Copper - chemistry Isotopes - chemistry Models, Chemical Nuclear Magnetic Resonance, Biomolecular Quantum Theory |
| title | Low Temperature 65Cu NMR Spectroscopy of the Cu+ Site in Azurin |
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