Electron Paramagnetic Resonance Studies of Cobalt-Copper Bovine Superoxide Dismutase
1. EPR spectra of cobalt-copper bovine superoxide dismutase at liquid nitrogen and liquid helium temperature show that the two metal centers are magnetically coupled. The temperature dependence of the spectra indicates that this coupling arises from an exchange interaction. 2. The EPR spectrum of th...
Gespeichert in:
| Veröffentlicht in: | The Journal of biological chemistry 1974-05, Vol.249 (10), p.3157-3160 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 3160 |
|---|---|
| container_issue | 10 |
| container_start_page | 3157 |
| container_title | The Journal of biological chemistry |
| container_volume | 249 |
| creator | Rotilio, Giuseppe Calabrese, Lilia Mondovì, Bruno Blumberg, William E. |
| description | 1. EPR spectra of cobalt-copper bovine superoxide dismutase at liquid nitrogen and liquid helium temperature show that the two metal centers are magnetically coupled. The temperature dependence of the spectra indicates that this coupling arises from an exchange interaction.
2. The EPR spectrum of the Co(II) of the enzyme can only be seen after reduction of the Cu(II), at very low temperature. It is typical of tetrahedral coordination which is distorted in a particular way. The EPR parameters are g⊥ ≃ 4, g|| ≃ 2, D = 11.5 cm-1. No feature indicating interaction between the two Co(II) centers is observed.
3. Anions such as CN- and N3- do not affect the EPR spectrum of Co(II) significantly, but only modify the spectrum of Cu(II).
It is concluded that the Co(II) site (and presumably the native Zn(II) site) can be described as distorted tetrahedral, strongly spin-coupled to the Cu(II) and therefore very near to it, and noninteracting with the other Co(II) site and with solvent molecules. |
| doi_str_mv | 10.1016/S0021-9258(19)42651-3 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_82381492</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0021925819426513</els_id><sourcerecordid>82381492</sourcerecordid><originalsourceid>FETCH-LOGICAL-c459t-f0c1e5bda8c2929a258ed133bdae503d9718fd6a116f1b32275a58c47968d4433</originalsourceid><addsrcrecordid>eNqFkE1v1DAQhi0EKtvCT6iIhITKIeCxnax9qmApH1IlENtK3CzHnuwaJfFiJwX-PU6z6hVfLM_7eGb0EHIO9A1QqN9uKWVQKlbJC1CvBasrKPkjsgIqeckr-PGYrB6Qp-Q0pZ80H6HghJwIXgsB9YrcXHVoxxiG4puJpje7AUdvi--YwmAGi8V2nJzHVIS22ITGdGO5CYcDxuJ9uPNDzqf8CH-8w-KDT_00moTPyJPWdAmfH-8zcvvx6mbzubz--unL5t11aUWlxrKlFrBqnJGWKaZM3hMdcJ4rWFHu1Bpk62oDULfQcMbWlamkFWtVSycE52fk1dL3EMOvCdOoe58sdp0ZMExJS8YlCMUyWC2gjSGliK0-RN-b-FcD1bNNfW9Tz6o0KH1vU88Dzo8DpqZH9_DrqC_nL5d873f73z6ibnywe-w1E2ruzaFaZ-rFQrUmaLOLPunbLaPA6RxLLjNxuRCYbd15jDpZj1m_yz3tqF3w_9n0HzFRmOo</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>82381492</pqid></control><display><type>article</type><title>Electron Paramagnetic Resonance Studies of Cobalt-Copper Bovine Superoxide Dismutase</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>Rotilio, Giuseppe ; Calabrese, Lilia ; Mondovì, Bruno ; Blumberg, William E.</creator><creatorcontrib>Rotilio, Giuseppe ; Calabrese, Lilia ; Mondovì, Bruno ; Blumberg, William E.</creatorcontrib><description>1. EPR spectra of cobalt-copper bovine superoxide dismutase at liquid nitrogen and liquid helium temperature show that the two metal centers are magnetically coupled. The temperature dependence of the spectra indicates that this coupling arises from an exchange interaction.
2. The EPR spectrum of the Co(II) of the enzyme can only be seen after reduction of the Cu(II), at very low temperature. It is typical of tetrahedral coordination which is distorted in a particular way. The EPR parameters are g⊥ ≃ 4, g|| ≃ 2, D = 11.5 cm-1. No feature indicating interaction between the two Co(II) centers is observed.
3. Anions such as CN- and N3- do not affect the EPR spectrum of Co(II) significantly, but only modify the spectrum of Cu(II).
It is concluded that the Co(II) site (and presumably the native Zn(II) site) can be described as distorted tetrahedral, strongly spin-coupled to the Cu(II) and therefore very near to it, and noninteracting with the other Co(II) site and with solvent molecules.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)42651-3</identifier><identifier>PMID: 4364416</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>animal science ; Azides ; Binding Sites ; Cobalt ; Cold Temperature ; Copper ; Cyanides ; Electron Spin Resonance Spectroscopy ; Ferrocyanides ; livestock ; Metalloproteins ; Oxidation-Reduction ; Protein Conformation ; Spectrophotometry ; Spectrophotometry, Ultraviolet ; Superoxide Dismutase ; Zinc ; zoology</subject><ispartof>The Journal of biological chemistry, 1974-05, Vol.249 (10), p.3157-3160</ispartof><rights>1974 © 1974 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c459t-f0c1e5bda8c2929a258ed133bdae503d9718fd6a116f1b32275a58c47968d4433</citedby><cites>FETCH-LOGICAL-c459t-f0c1e5bda8c2929a258ed133bdae503d9718fd6a116f1b32275a58c47968d4433</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4364416$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rotilio, Giuseppe</creatorcontrib><creatorcontrib>Calabrese, Lilia</creatorcontrib><creatorcontrib>Mondovì, Bruno</creatorcontrib><creatorcontrib>Blumberg, William E.</creatorcontrib><title>Electron Paramagnetic Resonance Studies of Cobalt-Copper Bovine Superoxide Dismutase</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>1. EPR spectra of cobalt-copper bovine superoxide dismutase at liquid nitrogen and liquid helium temperature show that the two metal centers are magnetically coupled. The temperature dependence of the spectra indicates that this coupling arises from an exchange interaction.
2. The EPR spectrum of the Co(II) of the enzyme can only be seen after reduction of the Cu(II), at very low temperature. It is typical of tetrahedral coordination which is distorted in a particular way. The EPR parameters are g⊥ ≃ 4, g|| ≃ 2, D = 11.5 cm-1. No feature indicating interaction between the two Co(II) centers is observed.
3. Anions such as CN- and N3- do not affect the EPR spectrum of Co(II) significantly, but only modify the spectrum of Cu(II).
It is concluded that the Co(II) site (and presumably the native Zn(II) site) can be described as distorted tetrahedral, strongly spin-coupled to the Cu(II) and therefore very near to it, and noninteracting with the other Co(II) site and with solvent molecules.</description><subject>animal science</subject><subject>Azides</subject><subject>Binding Sites</subject><subject>Cobalt</subject><subject>Cold Temperature</subject><subject>Copper</subject><subject>Cyanides</subject><subject>Electron Spin Resonance Spectroscopy</subject><subject>Ferrocyanides</subject><subject>livestock</subject><subject>Metalloproteins</subject><subject>Oxidation-Reduction</subject><subject>Protein Conformation</subject><subject>Spectrophotometry</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Superoxide Dismutase</subject><subject>Zinc</subject><subject>zoology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1974</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1v1DAQhi0EKtvCT6iIhITKIeCxnax9qmApH1IlENtK3CzHnuwaJfFiJwX-PU6z6hVfLM_7eGb0EHIO9A1QqN9uKWVQKlbJC1CvBasrKPkjsgIqeckr-PGYrB6Qp-Q0pZ80H6HghJwIXgsB9YrcXHVoxxiG4puJpje7AUdvi--YwmAGi8V2nJzHVIS22ITGdGO5CYcDxuJ9uPNDzqf8CH-8w-KDT_00moTPyJPWdAmfH-8zcvvx6mbzubz--unL5t11aUWlxrKlFrBqnJGWKaZM3hMdcJ4rWFHu1Bpk62oDULfQcMbWlamkFWtVSycE52fk1dL3EMOvCdOoe58sdp0ZMExJS8YlCMUyWC2gjSGliK0-RN-b-FcD1bNNfW9Tz6o0KH1vU88Dzo8DpqZH9_DrqC_nL5d873f73z6ibnywe-w1E2ruzaFaZ-rFQrUmaLOLPunbLaPA6RxLLjNxuRCYbd15jDpZj1m_yz3tqF3w_9n0HzFRmOo</recordid><startdate>19740525</startdate><enddate>19740525</enddate><creator>Rotilio, Giuseppe</creator><creator>Calabrese, Lilia</creator><creator>Mondovì, Bruno</creator><creator>Blumberg, William E.</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19740525</creationdate><title>Electron Paramagnetic Resonance Studies of Cobalt-Copper Bovine Superoxide Dismutase</title><author>Rotilio, Giuseppe ; Calabrese, Lilia ; Mondovì, Bruno ; Blumberg, William E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c459t-f0c1e5bda8c2929a258ed133bdae503d9718fd6a116f1b32275a58c47968d4433</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1974</creationdate><topic>animal science</topic><topic>Azides</topic><topic>Binding Sites</topic><topic>Cobalt</topic><topic>Cold Temperature</topic><topic>Copper</topic><topic>Cyanides</topic><topic>Electron Spin Resonance Spectroscopy</topic><topic>Ferrocyanides</topic><topic>livestock</topic><topic>Metalloproteins</topic><topic>Oxidation-Reduction</topic><topic>Protein Conformation</topic><topic>Spectrophotometry</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Superoxide Dismutase</topic><topic>Zinc</topic><topic>zoology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rotilio, Giuseppe</creatorcontrib><creatorcontrib>Calabrese, Lilia</creatorcontrib><creatorcontrib>Mondovì, Bruno</creatorcontrib><creatorcontrib>Blumberg, William E.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rotilio, Giuseppe</au><au>Calabrese, Lilia</au><au>Mondovì, Bruno</au><au>Blumberg, William E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Electron Paramagnetic Resonance Studies of Cobalt-Copper Bovine Superoxide Dismutase</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1974-05-25</date><risdate>1974</risdate><volume>249</volume><issue>10</issue><spage>3157</spage><epage>3160</epage><pages>3157-3160</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>1. EPR spectra of cobalt-copper bovine superoxide dismutase at liquid nitrogen and liquid helium temperature show that the two metal centers are magnetically coupled. The temperature dependence of the spectra indicates that this coupling arises from an exchange interaction.
2. The EPR spectrum of the Co(II) of the enzyme can only be seen after reduction of the Cu(II), at very low temperature. It is typical of tetrahedral coordination which is distorted in a particular way. The EPR parameters are g⊥ ≃ 4, g|| ≃ 2, D = 11.5 cm-1. No feature indicating interaction between the two Co(II) centers is observed.
3. Anions such as CN- and N3- do not affect the EPR spectrum of Co(II) significantly, but only modify the spectrum of Cu(II).
It is concluded that the Co(II) site (and presumably the native Zn(II) site) can be described as distorted tetrahedral, strongly spin-coupled to the Cu(II) and therefore very near to it, and noninteracting with the other Co(II) site and with solvent molecules.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>4364416</pmid><doi>10.1016/S0021-9258(19)42651-3</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1974-05, Vol.249 (10), p.3157-3160 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_82381492 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | animal science Azides Binding Sites Cobalt Cold Temperature Copper Cyanides Electron Spin Resonance Spectroscopy Ferrocyanides livestock Metalloproteins Oxidation-Reduction Protein Conformation Spectrophotometry Spectrophotometry, Ultraviolet Superoxide Dismutase Zinc zoology |
| title | Electron Paramagnetic Resonance Studies of Cobalt-Copper Bovine Superoxide Dismutase |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-27T10%3A19%3A10IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Electron%20Paramagnetic%20Resonance%20Studies%20of%20Cobalt-Copper%20Bovine%20Superoxide%20Dismutase&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Rotilio,%20Giuseppe&rft.date=1974-05-25&rft.volume=249&rft.issue=10&rft.spage=3157&rft.epage=3160&rft.pages=3157-3160&rft.issn=0021-9258&rft.eissn=1083-351X&rft_id=info:doi/10.1016/S0021-9258(19)42651-3&rft_dat=%3Cproquest_cross%3E82381492%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=82381492&rft_id=info:pmid/4364416&rft_els_id=S0021925819426513&rfr_iscdi=true |