Cytochrome c oxidase is three‐copper, two‐heme‐A protein
Metal contents of preparations of procaryotic (Paracoccus denitrificans) and eucaryotic (beef heart) cytochome c oxidases have been determined by inductively coupled plasma atomic emission spectroscopy and shown to be stoichiometrically related to the protein contents. The results show that oxidases...
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| Veröffentlicht in: | European journal of biochemistry 1987-04, Vol.164 (2), p.295-300 |
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| container_title | European journal of biochemistry |
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| creator | STEFFENS, Guy C. M. BIEWALD, Rosemarie BUSE, Gerhard |
| description | Metal contents of preparations of procaryotic (Paracoccus denitrificans) and eucaryotic (beef heart) cytochome c oxidases have been determined by inductively coupled plasma atomic emission spectroscopy and shown to be stoichiometrically related to the protein contents. The results show that oxidases which possess subunits I and II have three copper atoms besides hemes a and a3 (Paracoccus denitrificans, Cu: 2.97 ± 0.08 and Fe: 2.09 ± 0.10; bovine heart, Cu: 2.83 ± 0.07 and Fe: 1.94 ± 0.12). Together with data reported for the c1aa3 oxidase from Thermus thermophilus, the following conclusions can be drawn. Subunit I binds two copper atoms and both hemes a and a3 and thus is the universal terminal oxidase of this spectral type. Subunit II binds one copper and functions as an electron conductor.
The mitochondrial respiratory complex IV binds, in addition to three copper and two hemes a, stoichiometric amounts of magnesium and zinc (bovine heart Mg: 0.98 ± 0.05 and Zn: 1.01 ± 0.04). |
| doi_str_mv | 10.1111/j.1432-1033.1987.tb11057.x |
| format | Article |
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The mitochondrial respiratory complex IV binds, in addition to three copper and two hemes a, stoichiometric amounts of magnesium and zinc (bovine heart Mg: 0.98 ± 0.05 and Zn: 1.01 ± 0.04).</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1987.tb11057.x</identifier><identifier>PMID: 3032614</identifier><identifier>CODEN: EJBCAI</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Animals ; Applied sciences ; Binding Sites ; Cattle ; Copper - metabolism ; cytochrome-c oxidase ; Electron Transport Complex IV - metabolism ; Exact sciences and technology ; heart ; Heme - metabolism ; metals ; Myocardium - enzymology ; Other techniques and industries ; Paracoccus denitrificans ; Paracoccus denitrificans - enzymology ; Protein Conformation</subject><ispartof>European journal of biochemistry, 1987-04, Vol.164 (2), p.295-300</ispartof><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4635-cace0d97469fed888ed7a41f9d74d9a6a45b8e43511b3d1f10391d76df00a71e3</citedby><cites>FETCH-LOGICAL-c4635-cace0d97469fed888ed7a41f9d74d9a6a45b8e43511b3d1f10391d76df00a71e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7560345$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3032614$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>STEFFENS, Guy C. M.</creatorcontrib><creatorcontrib>BIEWALD, Rosemarie</creatorcontrib><creatorcontrib>BUSE, Gerhard</creatorcontrib><title>Cytochrome c oxidase is three‐copper, two‐heme‐A protein</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>Metal contents of preparations of procaryotic (Paracoccus denitrificans) and eucaryotic (beef heart) cytochome c oxidases have been determined by inductively coupled plasma atomic emission spectroscopy and shown to be stoichiometrically related to the protein contents. The results show that oxidases which possess subunits I and II have three copper atoms besides hemes a and a3 (Paracoccus denitrificans, Cu: 2.97 ± 0.08 and Fe: 2.09 ± 0.10; bovine heart, Cu: 2.83 ± 0.07 and Fe: 1.94 ± 0.12). Together with data reported for the c1aa3 oxidase from Thermus thermophilus, the following conclusions can be drawn. Subunit I binds two copper atoms and both hemes a and a3 and thus is the universal terminal oxidase of this spectral type. Subunit II binds one copper and functions as an electron conductor.
The mitochondrial respiratory complex IV binds, in addition to three copper and two hemes a, stoichiometric amounts of magnesium and zinc (bovine heart Mg: 0.98 ± 0.05 and Zn: 1.01 ± 0.04).</description><subject>Animals</subject><subject>Applied sciences</subject><subject>Binding Sites</subject><subject>Cattle</subject><subject>Copper - metabolism</subject><subject>cytochrome-c oxidase</subject><subject>Electron Transport Complex IV - metabolism</subject><subject>Exact sciences and technology</subject><subject>heart</subject><subject>Heme - metabolism</subject><subject>metals</subject><subject>Myocardium - enzymology</subject><subject>Other techniques and industries</subject><subject>Paracoccus denitrificans</subject><subject>Paracoccus denitrificans - enzymology</subject><subject>Protein Conformation</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkdFq2zAUhsXo6NJujzAwo-yq9nQsWbJ60ZGGthsUdrH2WijSMXGw40xySHLXR9gz9kkqE5PbUt0I6f-OzuETId-AZhDXj2UGnOUpUMYyUKXM-jkALWS2-0Amx-iETCgFnuaqEJ_IWQhLSqlQQp6SU0ZZLoBPyPVs33d24bsWE5t0u9qZgEkdkn7hEV-e_9tuvUZ_mfTbLp4W2A6X02Ttux7r1WfysTJNwC_jfk6e7m4fZ7_Shz_3v2fTh9RywYrUGovUKcmFqtCVZYlOGg6VcpI7ZYThxbxEzgqAOXNQxfEVOClcRamRgOycfD-8G_v-22DodVsHi01jVthtgpaSy1Ll5Zsg8BIKxXkErw6g9V0IHiu99nVr_F4D1YNlvdSDSj2o1INlPVrWu1j8deyymbfojqWj1phfjLkJ1jSVNytbhyMmC0EZLyL284Bt6wb37xhA393e_I3_yl4BlyWbdA</recordid><startdate>198704</startdate><enddate>198704</enddate><creator>STEFFENS, Guy C. M.</creator><creator>BIEWALD, Rosemarie</creator><creator>BUSE, Gerhard</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><scope>IQODW</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>198704</creationdate><title>Cytochrome c oxidase is three‐copper, two‐heme‐A protein</title><author>STEFFENS, Guy C. M. ; BIEWALD, Rosemarie ; BUSE, Gerhard</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4635-cace0d97469fed888ed7a41f9d74d9a6a45b8e43511b3d1f10391d76df00a71e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Animals</topic><topic>Applied sciences</topic><topic>Binding Sites</topic><topic>Cattle</topic><topic>Copper - metabolism</topic><topic>cytochrome-c oxidase</topic><topic>Electron Transport Complex IV - metabolism</topic><topic>Exact sciences and technology</topic><topic>heart</topic><topic>Heme - metabolism</topic><topic>metals</topic><topic>Myocardium - enzymology</topic><topic>Other techniques and industries</topic><topic>Paracoccus denitrificans</topic><topic>Paracoccus denitrificans - enzymology</topic><topic>Protein Conformation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>STEFFENS, Guy C. M.</creatorcontrib><creatorcontrib>BIEWALD, Rosemarie</creatorcontrib><creatorcontrib>BUSE, Gerhard</creatorcontrib><collection>Pascal-Francis</collection><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><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>STEFFENS, Guy C. M.</au><au>BIEWALD, Rosemarie</au><au>BUSE, Gerhard</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cytochrome c oxidase is three‐copper, two‐heme‐A protein</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1987-04</date><risdate>1987</risdate><volume>164</volume><issue>2</issue><spage>295</spage><epage>300</epage><pages>295-300</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><coden>EJBCAI</coden><abstract>Metal contents of preparations of procaryotic (Paracoccus denitrificans) and eucaryotic (beef heart) cytochome c oxidases have been determined by inductively coupled plasma atomic emission spectroscopy and shown to be stoichiometrically related to the protein contents. The results show that oxidases which possess subunits I and II have three copper atoms besides hemes a and a3 (Paracoccus denitrificans, Cu: 2.97 ± 0.08 and Fe: 2.09 ± 0.10; bovine heart, Cu: 2.83 ± 0.07 and Fe: 1.94 ± 0.12). Together with data reported for the c1aa3 oxidase from Thermus thermophilus, the following conclusions can be drawn. Subunit I binds two copper atoms and both hemes a and a3 and thus is the universal terminal oxidase of this spectral type. Subunit II binds one copper and functions as an electron conductor.
The mitochondrial respiratory complex IV binds, in addition to three copper and two hemes a, stoichiometric amounts of magnesium and zinc (bovine heart Mg: 0.98 ± 0.05 and Zn: 1.01 ± 0.04).</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>3032614</pmid><doi>10.1111/j.1432-1033.1987.tb11057.x</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | European journal of biochemistry, 1987-04, Vol.164 (2), p.295-300 |
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| language | eng |
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| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Animals Applied sciences Binding Sites Cattle Copper - metabolism cytochrome-c oxidase Electron Transport Complex IV - metabolism Exact sciences and technology heart Heme - metabolism metals Myocardium - enzymology Other techniques and industries Paracoccus denitrificans Paracoccus denitrificans - enzymology Protein Conformation |
| title | Cytochrome c oxidase is three‐copper, two‐heme‐A protein |
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