A conserved haem redox and trafficking pathway for cofactor attachment
A pathway for cytochrome c maturation (Ccm) in bacteria, archaea and eukaryotes (mitochondria) requires the genes encoding eight membrane proteins (CcmABCDEFGH). The CcmABCDE proteins are proposed to traffic haem to the cytochrome c synthetase (CcmF/H) for covalent attachment to cytochrome c by unkn...
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| Veröffentlicht in: | The EMBO journal 2009-08, Vol.28 (16), p.2349-2359 |
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| creator | Richard-Fogal, Cynthia L Frawley, Elaine R Bonner, Eric R Zhu, Huifen San Francisco, Brian Kranz, Robert G |
| description | A pathway for cytochrome
c
maturation (Ccm) in bacteria, archaea and eukaryotes (mitochondria) requires the genes encoding eight membrane proteins (CcmABCDEFGH). The CcmABCDE proteins are proposed to traffic haem to the cytochrome
c
synthetase (CcmF/H) for covalent attachment to cytochrome
c
by unknown mechanisms. For the first time, we purify pathway complexes with trapped haem to elucidate the molecular mechanisms of haem binding, trafficking and redox control. We discovered an early step in trafficking that involves oxidation of haem (to Fe
3+
), yet the final attachment requires reduced haem (Fe
2+
). Surprisingly, CcmF is a cytochrome
b
with a haem never before realized, and
in vitro
, CcmF functions as a quinol:haem oxidoreductase. Thus, this ancient pathway has conserved and orchestrated mechanisms for trafficking, storing and reducing haem, which assure its use for cytochrome
c
synthesis even in limiting haem (iron) environments and reducing haem in oxidizing environments. |
| doi_str_mv | 10.1038/emboj.2009.189 |
| format | Article |
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c
maturation (Ccm) in bacteria, archaea and eukaryotes (mitochondria) requires the genes encoding eight membrane proteins (CcmABCDEFGH). The CcmABCDE proteins are proposed to traffic haem to the cytochrome
c
synthetase (CcmF/H) for covalent attachment to cytochrome
c
by unknown mechanisms. For the first time, we purify pathway complexes with trapped haem to elucidate the molecular mechanisms of haem binding, trafficking and redox control. We discovered an early step in trafficking that involves oxidation of haem (to Fe
3+
), yet the final attachment requires reduced haem (Fe
2+
). Surprisingly, CcmF is a cytochrome
b
with a haem never before realized, and
in vitro
, CcmF functions as a quinol:haem oxidoreductase. Thus, this ancient pathway has conserved and orchestrated mechanisms for trafficking, storing and reducing haem, which assure its use for cytochrome
c
synthesis even in limiting haem (iron) environments and reducing haem in oxidizing environments.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1038/emboj.2009.189</identifier><identifier>PMID: 19629033</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Amino Acid Sequence ; Archaea ; Bacterial Outer Membrane Proteins - genetics ; Bacterial Outer Membrane Proteins - isolation & purification ; Bacterial Outer Membrane Proteins - metabolism ; Binding Sites ; Cytochrome ; Cytochromes c - metabolism ; EMBO20 ; EMBO31 ; Escherichia coli - enzymology ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Escherichia coli Proteins - genetics ; Escherichia coli Proteins - isolation & purification ; Escherichia coli Proteins - metabolism ; Genetics ; haem ; Heme - isolation & purification ; Heme - metabolism ; Hemeproteins - isolation & purification ; Hemeproteins - metabolism ; Hydroquinones - metabolism ; Iron - metabolism ; Lyases - genetics ; Lyases - isolation & purification ; Lyases - metabolism ; Membranes ; Molecular biology ; Oxidation ; Oxidation-Reduction ; Protein Binding ; Proteins ; quinone ; redox ; Trafficking</subject><ispartof>The EMBO journal, 2009-08, Vol.28 (16), p.2349-2359</ispartof><rights>European Molecular Biology Organization 2009</rights><rights>Copyright © 2009 European Molecular Biology Organization</rights><rights>Copyright Nature Publishing Group Aug 19, 2009</rights><rights>Copyright © 2009, European Molecular Biology Organization 2009</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5999-fc99b65c04ca81b35a27e7bf13ae0bc18c1f3b5d26326457195ac33bc7b7738d3</citedby><cites>FETCH-LOGICAL-c5999-fc99b65c04ca81b35a27e7bf13ae0bc18c1f3b5d26326457195ac33bc7b7738d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2735175/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2735175/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1416,1432,27923,27924,41119,42188,45573,45574,46408,46832,51575,53790,53792</link.rule.ids><linktorsrc>$$Uhttps://doi.org/10.1038/emboj.2009.189$$EView_record_in_Springer_Nature$$FView_record_in_$$GSpringer_Nature</linktorsrc><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19629033$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Richard-Fogal, Cynthia L</creatorcontrib><creatorcontrib>Frawley, Elaine R</creatorcontrib><creatorcontrib>Bonner, Eric R</creatorcontrib><creatorcontrib>Zhu, Huifen</creatorcontrib><creatorcontrib>San Francisco, Brian</creatorcontrib><creatorcontrib>Kranz, Robert G</creatorcontrib><title>A conserved haem redox and trafficking pathway for cofactor attachment</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>A pathway for cytochrome
c
maturation (Ccm) in bacteria, archaea and eukaryotes (mitochondria) requires the genes encoding eight membrane proteins (CcmABCDEFGH). The CcmABCDE proteins are proposed to traffic haem to the cytochrome
c
synthetase (CcmF/H) for covalent attachment to cytochrome
c
by unknown mechanisms. For the first time, we purify pathway complexes with trapped haem to elucidate the molecular mechanisms of haem binding, trafficking and redox control. We discovered an early step in trafficking that involves oxidation of haem (to Fe
3+
), yet the final attachment requires reduced haem (Fe
2+
). Surprisingly, CcmF is a cytochrome
b
with a haem never before realized, and
in vitro
, CcmF functions as a quinol:haem oxidoreductase. Thus, this ancient pathway has conserved and orchestrated mechanisms for trafficking, storing and reducing haem, which assure its use for cytochrome
c
synthesis even in limiting haem (iron) environments and reducing haem in oxidizing environments.</description><subject>Amino Acid Sequence</subject><subject>Archaea</subject><subject>Bacterial Outer Membrane Proteins - genetics</subject><subject>Bacterial Outer Membrane Proteins - isolation & purification</subject><subject>Bacterial Outer Membrane Proteins - metabolism</subject><subject>Binding Sites</subject><subject>Cytochrome</subject><subject>Cytochromes c - metabolism</subject><subject>EMBO20</subject><subject>EMBO31</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins - genetics</subject><subject>Escherichia coli Proteins - isolation & purification</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Genetics</subject><subject>haem</subject><subject>Heme - isolation & purification</subject><subject>Heme - metabolism</subject><subject>Hemeproteins - isolation & purification</subject><subject>Hemeproteins - metabolism</subject><subject>Hydroquinones - metabolism</subject><subject>Iron - metabolism</subject><subject>Lyases - genetics</subject><subject>Lyases - isolation & purification</subject><subject>Lyases - metabolism</subject><subject>Membranes</subject><subject>Molecular biology</subject><subject>Oxidation</subject><subject>Oxidation-Reduction</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>quinone</subject><subject>redox</subject><subject>Trafficking</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkd1v0zAUxS0EYmXjlUcU8cBbOjuuY_sFaUxbYQz2IRASL9aN47TpkrjYzrb-97hN1Q0ktCd__e655_og9IbgMcFUHJq2sItxhrEcEyGfoRGZ5DjNMGfP0QhnOUkn8X4PvfJ-gTFmgpOXaI_IPJOY0hE6PUq07bxxt6ZM5mDaxJnS3ifQlUlwUFW1vqm7WbKEML-DVVJZFwsq0CFuIATQ89Z04QC9qKDx5vV23Uc_Tk--H39Kzy-mn4-PzlPNpJRppaUscqbxRIMgBWWQccOLilAwuNBEaFLRgpVZTrN8wjiRDDSlheYF51SUdB99GHSXfdGaUsfWDhq1dHULbqUs1Orvl66eq5m9VRmnjHAWBd5vBZz93RsfVFt7bZoGOmN7r3LOZC44fRLMsMBEbBTf_QMubO-6-Asq2o9jSCIiNB4g7az3zlQ7ywSrdZBqE6RaB6liYLHg7eNBH_BtchHgA3BXN2b1hJw6-frxbH0YpA-HSh-Luplxjwz_z8x2xA5C78yu2QZ7kE0HqPbB3O8YcDfxUyln6ue3qZpefrm6vjr7pab0D7no1nw</recordid><startdate>20090819</startdate><enddate>20090819</enddate><creator>Richard-Fogal, Cynthia L</creator><creator>Frawley, Elaine R</creator><creator>Bonner, Eric R</creator><creator>Zhu, Huifen</creator><creator>San Francisco, Brian</creator><creator>Kranz, Robert G</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><general>Nature Publishing Group</general><scope>BSCLL</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>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20090819</creationdate><title>A conserved haem redox and trafficking pathway for cofactor attachment</title><author>Richard-Fogal, Cynthia L ; Frawley, Elaine R ; Bonner, Eric R ; Zhu, Huifen ; San Francisco, Brian ; Kranz, Robert G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5999-fc99b65c04ca81b35a27e7bf13ae0bc18c1f3b5d26326457195ac33bc7b7738d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Amino Acid Sequence</topic><topic>Archaea</topic><topic>Bacterial Outer Membrane Proteins - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Richard-Fogal, Cynthia L</au><au>Frawley, Elaine R</au><au>Bonner, Eric R</au><au>Zhu, Huifen</au><au>San Francisco, Brian</au><au>Kranz, Robert G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A conserved haem redox and trafficking pathway for cofactor attachment</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2009-08-19</date><risdate>2009</risdate><volume>28</volume><issue>16</issue><spage>2349</spage><epage>2359</epage><pages>2349-2359</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>A pathway for cytochrome
c
maturation (Ccm) in bacteria, archaea and eukaryotes (mitochondria) requires the genes encoding eight membrane proteins (CcmABCDEFGH). The CcmABCDE proteins are proposed to traffic haem to the cytochrome
c
synthetase (CcmF/H) for covalent attachment to cytochrome
c
by unknown mechanisms. For the first time, we purify pathway complexes with trapped haem to elucidate the molecular mechanisms of haem binding, trafficking and redox control. We discovered an early step in trafficking that involves oxidation of haem (to Fe
3+
), yet the final attachment requires reduced haem (Fe
2+
). Surprisingly, CcmF is a cytochrome
b
with a haem never before realized, and
in vitro
, CcmF functions as a quinol:haem oxidoreductase. Thus, this ancient pathway has conserved and orchestrated mechanisms for trafficking, storing and reducing haem, which assure its use for cytochrome
c
synthesis even in limiting haem (iron) environments and reducing haem in oxidizing environments.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>19629033</pmid><doi>10.1038/emboj.2009.189</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0261-4189 |
| ispartof | The EMBO journal, 2009-08, Vol.28 (16), p.2349-2359 |
| issn | 0261-4189 1460-2075 |
| language | eng |
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| source | Springer Nature OA Free Journals |
| subjects | Amino Acid Sequence Archaea Bacterial Outer Membrane Proteins - genetics Bacterial Outer Membrane Proteins - isolation & purification Bacterial Outer Membrane Proteins - metabolism Binding Sites Cytochrome Cytochromes c - metabolism EMBO20 EMBO31 Escherichia coli - enzymology Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins - genetics Escherichia coli Proteins - isolation & purification Escherichia coli Proteins - metabolism Genetics haem Heme - isolation & purification Heme - metabolism Hemeproteins - isolation & purification Hemeproteins - metabolism Hydroquinones - metabolism Iron - metabolism Lyases - genetics Lyases - isolation & purification Lyases - metabolism Membranes Molecular biology Oxidation Oxidation-Reduction Protein Binding Proteins quinone redox Trafficking |
| title | A conserved haem redox and trafficking pathway for cofactor attachment |
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