Copper metallochaperones
The current state of knowledge on how copper metallochaperones support the maturation of cuproproteins is reviewed. Copper is needed within mitochondria to supply the Cu(A) and intramembrane Cu(B) sites of cytochrome oxidase, within the trans-Golgi network to supply secreted cuproproteins and within...
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| Veröffentlicht in: | Annual review of biochemistry 2010-01, Vol.79 (1), p.537-562 |
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| creator | Robinson, Nigel J Winge, Dennis R |
| description | The current state of knowledge on how copper metallochaperones support the maturation of cuproproteins is reviewed. Copper is needed within mitochondria to supply the Cu(A) and intramembrane Cu(B) sites of cytochrome oxidase, within the trans-Golgi network to supply secreted cuproproteins and within the cytosol to supply superoxide dismutase 1 (Sod1). Subpopulations of copper-zinc superoxide dismutase also localize to mitochondria, the secretory system, the nucleus and, in plants, the chloroplast, which also requires copper for plastocyanin. Prokaryotic cuproproteins are found in the cell membrane and in the periplasm of gram-negative bacteria. Cu(I) and Cu(II) form tight complexes with organic molecules and drive redox chemistry, which unrestrained would be destructive. Copper metallochaperones assist copper in reaching vital destinations without inflicting damage or becoming trapped in adventitious binding sites. Copper ions are specifically released from copper metallochaperones upon contact with their cognate cuproproteins and metal transfer is thought to proceed by ligand substitution. |
| doi_str_mv | 10.1146/annurev-biochem-030409-143539 |
| format | Article |
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Copper is needed within mitochondria to supply the Cu(A) and intramembrane Cu(B) sites of cytochrome oxidase, within the trans-Golgi network to supply secreted cuproproteins and within the cytosol to supply superoxide dismutase 1 (Sod1). Subpopulations of copper-zinc superoxide dismutase also localize to mitochondria, the secretory system, the nucleus and, in plants, the chloroplast, which also requires copper for plastocyanin. Prokaryotic cuproproteins are found in the cell membrane and in the periplasm of gram-negative bacteria. Cu(I) and Cu(II) form tight complexes with organic molecules and drive redox chemistry, which unrestrained would be destructive. Copper metallochaperones assist copper in reaching vital destinations without inflicting damage or becoming trapped in adventitious binding sites. Copper ions are specifically released from copper metallochaperones upon contact with their cognate cuproproteins and metal transfer is thought to proceed by ligand substitution.</description><identifier>ISSN: 0066-4154</identifier><identifier>EISSN: 1545-4509</identifier><identifier>DOI: 10.1146/annurev-biochem-030409-143539</identifier><identifier>PMID: 20205585</identifier><identifier>CODEN: ARBOAW</identifier><language>eng</language><publisher>United States: Annual Reviews, Inc</publisher><subject>Bacteria ; Bacteria - metabolism ; Biochemistry ; Cation Transport Proteins - chemistry ; Cation Transport Proteins - metabolism ; Copper ; Copper - metabolism ; Cytosol - metabolism ; Eukaryotic Cells - metabolism ; Maturation ; Metallochaperones - chemistry ; Metallochaperones - metabolism ; Mitochondria ; Mitochondria - metabolism ; Oxidation ; Prokaryotes ; Proteins ; Proteome - analysis ; Subpopulations</subject><ispartof>Annual review of biochemistry, 2010-01, Vol.79 (1), p.537-562</ispartof><rights>Copyright Annual Reviews, Inc. 2010</rights><rights>Copyright © 2010 by Annual Reviews. 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Copper is needed within mitochondria to supply the Cu(A) and intramembrane Cu(B) sites of cytochrome oxidase, within the trans-Golgi network to supply secreted cuproproteins and within the cytosol to supply superoxide dismutase 1 (Sod1). Subpopulations of copper-zinc superoxide dismutase also localize to mitochondria, the secretory system, the nucleus and, in plants, the chloroplast, which also requires copper for plastocyanin. Prokaryotic cuproproteins are found in the cell membrane and in the periplasm of gram-negative bacteria. Cu(I) and Cu(II) form tight complexes with organic molecules and drive redox chemistry, which unrestrained would be destructive. Copper metallochaperones assist copper in reaching vital destinations without inflicting damage or becoming trapped in adventitious binding sites. Copper ions are specifically released from copper metallochaperones upon contact with their cognate cuproproteins and metal transfer is thought to proceed by ligand substitution.</description><subject>Bacteria</subject><subject>Bacteria - metabolism</subject><subject>Biochemistry</subject><subject>Cation Transport Proteins - chemistry</subject><subject>Cation Transport Proteins - metabolism</subject><subject>Copper</subject><subject>Copper - metabolism</subject><subject>Cytosol - metabolism</subject><subject>Eukaryotic Cells - metabolism</subject><subject>Maturation</subject><subject>Metallochaperones - chemistry</subject><subject>Metallochaperones - metabolism</subject><subject>Mitochondria</subject><subject>Mitochondria - metabolism</subject><subject>Oxidation</subject><subject>Prokaryotes</subject><subject>Proteins</subject><subject>Proteome - analysis</subject><subject>Subpopulations</subject><issn>0066-4154</issn><issn>1545-4509</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkU1LxDAQhoMouq7ePYkI4qk6bTJpc1CQxS9Y8KLnkGRTt0vbrEm74L830rqopzDJMy8zeQi5SOEqTRm_Vm3be7tJdOXM0jYJUGAgkpRRpGKHTFJkmDAEsUsmAJwnLN4ckMMQVgBABcv2yUEGGSAWOCEnM7deW3_W2E7VdYxUsXKtDUdkr1R1sMfjOSVvD_evs6dk_vL4PLubJ4oz7BJqIAeLaDXNreZYcq04zYsCUmOA5VgynWlQHHGhKRpWUjCG8VyXqmSxmpLbIXfd68YujG07r2q59lWj_Kd0qpJ_X9pqKd_dRlJR8AKKGHA5Bnj30dvQyaYKxta1aq3rg8wpzXgW0Uie_yNXrvdt3E4i5IUALkSEbgbIeBeCt-V2lBTktwE5GpCjATkYkIOB2H_6e59t98-X0y-E9ocQ</recordid><startdate>20100101</startdate><enddate>20100101</enddate><creator>Robinson, Nigel J</creator><creator>Winge, Dennis R</creator><general>Annual Reviews, 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>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20100101</creationdate><title>Copper metallochaperones</title><author>Robinson, Nigel J ; 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Copper is needed within mitochondria to supply the Cu(A) and intramembrane Cu(B) sites of cytochrome oxidase, within the trans-Golgi network to supply secreted cuproproteins and within the cytosol to supply superoxide dismutase 1 (Sod1). Subpopulations of copper-zinc superoxide dismutase also localize to mitochondria, the secretory system, the nucleus and, in plants, the chloroplast, which also requires copper for plastocyanin. Prokaryotic cuproproteins are found in the cell membrane and in the periplasm of gram-negative bacteria. Cu(I) and Cu(II) form tight complexes with organic molecules and drive redox chemistry, which unrestrained would be destructive. Copper metallochaperones assist copper in reaching vital destinations without inflicting damage or becoming trapped in adventitious binding sites. Copper ions are specifically released from copper metallochaperones upon contact with their cognate cuproproteins and metal transfer is thought to proceed by ligand substitution.</abstract><cop>United States</cop><pub>Annual Reviews, Inc</pub><pmid>20205585</pmid><doi>10.1146/annurev-biochem-030409-143539</doi><tpages>26</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Bacteria Bacteria - metabolism Biochemistry Cation Transport Proteins - chemistry Cation Transport Proteins - metabolism Copper Copper - metabolism Cytosol - metabolism Eukaryotic Cells - metabolism Maturation Metallochaperones - chemistry Metallochaperones - metabolism Mitochondria Mitochondria - metabolism Oxidation Prokaryotes Proteins Proteome - analysis Subpopulations |
| title | Copper metallochaperones |
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