CzcE from Cupriavidus metallidurans CH34 is a copper-binding protein
CzcE is encoded by the most distal gene of the czc determinant that allows Cupriavidus metallidurans CH34 to modulate its internal concentrations of cobalt, zinc and cadmium by regulation of the expression of the efflux pump CzcCBA. We have overproduced and purified CzcE. CzcE is a periplasm-located...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2008-01, Vol.365 (4), p.735-739 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Zoropogui, Anthony Gambarelli, Serge Covès, Jacques |
| description | CzcE is encoded by the most distal gene of the
czc determinant that allows
Cupriavidus metallidurans CH34 to modulate its internal concentrations of cobalt, zinc and cadmium by regulation of the expression of the efflux pump CzcCBA. We have overproduced and purified CzcE. CzcE is a periplasm-located dimeric protein able to bind specifically 4 Cu-equivalent per dimer. Spectrophotometry and EPR are indicative of type II copper with typical d–d transitions. Re-oxidation of fully reduced CzcE led to the formation of an air stable semi-reduced form binding both 2 Cu(I) and 2 Cu(II) ions. The spectroscopic characteristics of the semi-reduced form are different of those of the oxidized one, suggesting a change in the environment of Cu(II). |
| doi_str_mv | 10.1016/j.bbrc.2007.11.030 |
| format | Article |
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czc determinant that allows
Cupriavidus metallidurans CH34 to modulate its internal concentrations of cobalt, zinc and cadmium by regulation of the expression of the efflux pump CzcCBA. We have overproduced and purified CzcE. CzcE is a periplasm-located dimeric protein able to bind specifically 4 Cu-equivalent per dimer. Spectrophotometry and EPR are indicative of type II copper with typical d–d transitions. Re-oxidation of fully reduced CzcE led to the formation of an air stable semi-reduced form binding both 2 Cu(I) and 2 Cu(II) ions. The spectroscopic characteristics of the semi-reduced form are different of those of the oxidized one, suggesting a change in the environment of Cu(II).</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2007.11.030</identifier><identifier>PMID: 18029263</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>60 APPLIED LIFE SCIENCES ; AIR ; Bacterial Proteins - chemistry ; Binding Sites ; CADMIUM ; COBALT ; COPPER ; Copper - chemistry ; COPPER IONS ; Cupriavidus - chemistry ; Cupriavidus metallidurans CH34 ; Czc determinant ; DIMERS ; ELECTRON SPIN RESONANCE ; GENES ; Heavy metal resistance ; HEAVY METALS ; Metal binding protein ; Protein Binding ; PROTEINS ; SPECTROPHOTOMETRY ; ZINC</subject><ispartof>Biochemical and biophysical research communications, 2008-01, Vol.365 (4), p.735-739</ispartof><rights>2007 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c413t-a686c75d979599d8ec0f610a79ab6671813c4882faaddf21095c8140663171233</citedby><cites>FETCH-LOGICAL-c413t-a686c75d979599d8ec0f610a79ab6671813c4882faaddf21095c8140663171233</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbrc.2007.11.030$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,780,784,885,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18029263$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/21043588$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Zoropogui, Anthony</creatorcontrib><creatorcontrib>Gambarelli, Serge</creatorcontrib><creatorcontrib>Covès, Jacques</creatorcontrib><title>CzcE from Cupriavidus metallidurans CH34 is a copper-binding protein</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>CzcE is encoded by the most distal gene of the
czc determinant that allows
Cupriavidus metallidurans CH34 to modulate its internal concentrations of cobalt, zinc and cadmium by regulation of the expression of the efflux pump CzcCBA. We have overproduced and purified CzcE. CzcE is a periplasm-located dimeric protein able to bind specifically 4 Cu-equivalent per dimer. Spectrophotometry and EPR are indicative of type II copper with typical d–d transitions. Re-oxidation of fully reduced CzcE led to the formation of an air stable semi-reduced form binding both 2 Cu(I) and 2 Cu(II) ions. The spectroscopic characteristics of the semi-reduced form are different of those of the oxidized one, suggesting a change in the environment of Cu(II).</description><subject>60 APPLIED LIFE SCIENCES</subject><subject>AIR</subject><subject>Bacterial Proteins - chemistry</subject><subject>Binding Sites</subject><subject>CADMIUM</subject><subject>COBALT</subject><subject>COPPER</subject><subject>Copper - chemistry</subject><subject>COPPER IONS</subject><subject>Cupriavidus - chemistry</subject><subject>Cupriavidus metallidurans CH34</subject><subject>Czc determinant</subject><subject>DIMERS</subject><subject>ELECTRON SPIN RESONANCE</subject><subject>GENES</subject><subject>Heavy metal resistance</subject><subject>HEAVY METALS</subject><subject>Metal binding protein</subject><subject>Protein Binding</subject><subject>PROTEINS</subject><subject>SPECTROPHOTOMETRY</subject><subject>ZINC</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtr3TAQhUVpaG7S_oEugqHQnZ0ZyZYlyCY4Twhkk0J3QpbkRhc_biU7kPz6ytwL3SWrmcU3hznnEPIdoUBAfr4t2jaYggLUBWIBDD6RDYKEnCKUn8kGAHhOJf4-JicxbgEQSy6_kGMUQCXlbEOumjdznXVhGrJm2QWvX7xdYja4Wfd9WoMeY9bcsTLzMdOZmXY7F_LWj9aPf7JdmGbnx6_kqNN9dN8O85T8url-au7yh8fb--byITclsjnXXHBTV1bWspLSCmeg4wi6lrrlvEaBzJRC0E5ra7vkQVZGYAmcM6yRMnZKfux1pzh7FY2fnXk20zg6M6vVM6uESNTPPZW--7u4OKvBR-P6Xo9uWqKqAQGkYB-CFDhFWlcJpHvQhCnG4DqVkhp0eFUIaq1CbdVahVqrUIgqVZGOzg7qSzs4-__kkH0CLvaAS5G9eBdWR240zvqwGrKTf0__H4wRlvU</recordid><startdate>20080125</startdate><enddate>20080125</enddate><creator>Zoropogui, Anthony</creator><creator>Gambarelli, Serge</creator><creator>Covès, Jacques</creator><general>Elsevier Inc</general><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>7QL</scope><scope>C1K</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>20080125</creationdate><title>CzcE from Cupriavidus metallidurans CH34 is a copper-binding protein</title><author>Zoropogui, Anthony ; Gambarelli, Serge ; Covès, Jacques</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c413t-a686c75d979599d8ec0f610a79ab6671813c4882faaddf21095c8140663171233</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>60 APPLIED LIFE SCIENCES</topic><topic>AIR</topic><topic>Bacterial Proteins - chemistry</topic><topic>Binding Sites</topic><topic>CADMIUM</topic><topic>COBALT</topic><topic>COPPER</topic><topic>Copper - chemistry</topic><topic>COPPER IONS</topic><topic>Cupriavidus - chemistry</topic><topic>Cupriavidus metallidurans CH34</topic><topic>Czc determinant</topic><topic>DIMERS</topic><topic>ELECTRON SPIN RESONANCE</topic><topic>GENES</topic><topic>Heavy metal resistance</topic><topic>HEAVY METALS</topic><topic>Metal binding protein</topic><topic>Protein Binding</topic><topic>PROTEINS</topic><topic>SPECTROPHOTOMETRY</topic><topic>ZINC</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zoropogui, Anthony</creatorcontrib><creatorcontrib>Gambarelli, Serge</creatorcontrib><creatorcontrib>Covès, Jacques</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zoropogui, Anthony</au><au>Gambarelli, Serge</au><au>Covès, Jacques</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>CzcE from Cupriavidus metallidurans CH34 is a copper-binding protein</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2008-01-25</date><risdate>2008</risdate><volume>365</volume><issue>4</issue><spage>735</spage><epage>739</epage><pages>735-739</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>CzcE is encoded by the most distal gene of the
czc determinant that allows
Cupriavidus metallidurans CH34 to modulate its internal concentrations of cobalt, zinc and cadmium by regulation of the expression of the efflux pump CzcCBA. We have overproduced and purified CzcE. CzcE is a periplasm-located dimeric protein able to bind specifically 4 Cu-equivalent per dimer. Spectrophotometry and EPR are indicative of type II copper with typical d–d transitions. Re-oxidation of fully reduced CzcE led to the formation of an air stable semi-reduced form binding both 2 Cu(I) and 2 Cu(II) ions. The spectroscopic characteristics of the semi-reduced form are different of those of the oxidized one, suggesting a change in the environment of Cu(II).</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>18029263</pmid><doi>10.1016/j.bbrc.2007.11.030</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Biochemical and biophysical research communications, 2008-01, Vol.365 (4), p.735-739 |
| issn | 0006-291X 1090-2104 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | 60 APPLIED LIFE SCIENCES AIR Bacterial Proteins - chemistry Binding Sites CADMIUM COBALT COPPER Copper - chemistry COPPER IONS Cupriavidus - chemistry Cupriavidus metallidurans CH34 Czc determinant DIMERS ELECTRON SPIN RESONANCE GENES Heavy metal resistance HEAVY METALS Metal binding protein Protein Binding PROTEINS SPECTROPHOTOMETRY ZINC |
| title | CzcE from Cupriavidus metallidurans CH34 is a copper-binding protein |
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