Supramolecular organizations in the aerobic respiratory chain of Escherichia coli
The organization of respiratory chain complexes in supercomplexes has been shown in the mitochondria of several eukaryotes and in the cell membranes of some bacteria. These supercomplexes are suggested to be important for oxidative phosphorylation efficiency and to prevent the formation of reactive...
Gespeichert in:
| Veröffentlicht in: | Biochimie 2011-03, Vol.93 (3), p.418-425 |
|---|---|
| Hauptverfasser: | , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 425 |
|---|---|
| container_issue | 3 |
| container_start_page | 418 |
| container_title | Biochimie |
| container_volume | 93 |
| creator | Sousa, Pedro M.F. Silva, Sara T.N. Hood, Brian L. Charro, Nuno Carita, João N. Vaz, Fátima Penque, Deborah Conrads, Thomas P. Melo, Ana M.P. |
| description | The organization of respiratory chain complexes in supercomplexes has been shown in the mitochondria of several eukaryotes and in the cell membranes of some bacteria. These supercomplexes are suggested to be important for oxidative phosphorylation efficiency and to prevent the formation of reactive oxygen species.
Here we describe, for the first time, the identification of supramolecular organizations in the aerobic respiratory chain of Escherichia coli, including a trimer of succinate dehydrogenase. Furthermore, two heterooligomerizations have been shown: one resulting from the association of the NADH:quinone oxidoreductases NDH-1 and NDH-2, and another composed by the cytochrome bo3 quinol:oxygen reductase, cytochrome bd quinol:oxygen reductase and formate dehydrogenase (fdo). These results are supported by blue native-electrophoresis, mass spectrometry and kinetic data of wild type and mutant E . coli strains.
► The E. coli respiratory chain is organized in supercomplexes. ► A formate dehydrogenase:oxygen reductase supercomplex was identified. ► NDH-1 and NDH-2 are associated in a supercomplex. |
| doi_str_mv | 10.1016/j.biochi.2010.10.014 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_888098220</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0300908410003743</els_id><sourcerecordid>851749618</sourcerecordid><originalsourceid>FETCH-LOGICAL-c505t-46073118293883f54f7210aff500f9860afda5759aef0107cde58ce190dbcbc3</originalsourceid><addsrcrecordid>eNqFkE1PwzAMhiMEYmPwDxDqjVOH0zZtekFC0_iQJiHE7lGaOixT14ykRRq_nowOjnCyZb_2az-EXFKYUqD5zXpaGatWZprAd2kKNDsiY5qnPM4pT4_JGFKAuASejciZ92sAYJCUp2SUUMigYOmYvLz2Wyc3tkHVN9JF1r3J1nzKztjWR6aNuhVGEp2tjIoc-q1xsrNuF6mVDF2ro7lXK3QmXCIjZRtzTk60bDxeHOKELO_ny9ljvHh-eJrdLWLFgHVxlkORUsqTMuU81SzTRbhKas0AdMnzkNaSFayUqMODhaqRcYW0hLpSlUon5HpYu3X2vUffiY3xCptGtmh7LzjnUPIkgf-VjBZZuUc2IdmgVM5671CLrTMb6XaCgthDF2sxQBd76PtqgB7Grg4GfbXB-nfoh3IQ3A4CDDw-DDrhlcFWYW0cqk7U1vzt8AXEA5TE</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>851749618</pqid></control><display><type>article</type><title>Supramolecular organizations in the aerobic respiratory chain of Escherichia coli</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Sousa, Pedro M.F. ; Silva, Sara T.N. ; Hood, Brian L. ; Charro, Nuno ; Carita, João N. ; Vaz, Fátima ; Penque, Deborah ; Conrads, Thomas P. ; Melo, Ana M.P.</creator><creatorcontrib>Sousa, Pedro M.F. ; Silva, Sara T.N. ; Hood, Brian L. ; Charro, Nuno ; Carita, João N. ; Vaz, Fátima ; Penque, Deborah ; Conrads, Thomas P. ; Melo, Ana M.P.</creatorcontrib><description>The organization of respiratory chain complexes in supercomplexes has been shown in the mitochondria of several eukaryotes and in the cell membranes of some bacteria. These supercomplexes are suggested to be important for oxidative phosphorylation efficiency and to prevent the formation of reactive oxygen species.
Here we describe, for the first time, the identification of supramolecular organizations in the aerobic respiratory chain of Escherichia coli, including a trimer of succinate dehydrogenase. Furthermore, two heterooligomerizations have been shown: one resulting from the association of the NADH:quinone oxidoreductases NDH-1 and NDH-2, and another composed by the cytochrome bo3 quinol:oxygen reductase, cytochrome bd quinol:oxygen reductase and formate dehydrogenase (fdo). These results are supported by blue native-electrophoresis, mass spectrometry and kinetic data of wild type and mutant E . coli strains.
► The E. coli respiratory chain is organized in supercomplexes. ► A formate dehydrogenase:oxygen reductase supercomplex was identified. ► NDH-1 and NDH-2 are associated in a supercomplex.</description><identifier>ISSN: 0300-9084</identifier><identifier>EISSN: 1638-6183</identifier><identifier>DOI: 10.1016/j.biochi.2010.10.014</identifier><identifier>PMID: 21040753</identifier><language>eng</language><publisher>France: Elsevier B.V</publisher><subject>Aerobic respiratory chain ; Aerobiosis ; Amino Acid Sequence ; Bioenergetics ; Cell Membrane - enzymology ; Cell Membrane - metabolism ; Electron Transport ; Electrophoresis ; Escherichia coli ; Escherichia coli K12 - cytology ; Escherichia coli K12 - enzymology ; Escherichia coli K12 - metabolism ; Molecular Sequence Data ; NADH:quinone oxidoreductase ; Oxygen reductase ; Protein Multimerization ; Protein Structure, Quaternary ; Solubility ; Supercomplex</subject><ispartof>Biochimie, 2011-03, Vol.93 (3), p.418-425</ispartof><rights>2010 Elsevier Masson SAS</rights><rights>Copyright © 2010 Elsevier Masson SAS. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c505t-46073118293883f54f7210aff500f9860afda5759aef0107cde58ce190dbcbc3</citedby><cites>FETCH-LOGICAL-c505t-46073118293883f54f7210aff500f9860afda5759aef0107cde58ce190dbcbc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0300908410003743$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21040753$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sousa, Pedro M.F.</creatorcontrib><creatorcontrib>Silva, Sara T.N.</creatorcontrib><creatorcontrib>Hood, Brian L.</creatorcontrib><creatorcontrib>Charro, Nuno</creatorcontrib><creatorcontrib>Carita, João N.</creatorcontrib><creatorcontrib>Vaz, Fátima</creatorcontrib><creatorcontrib>Penque, Deborah</creatorcontrib><creatorcontrib>Conrads, Thomas P.</creatorcontrib><creatorcontrib>Melo, Ana M.P.</creatorcontrib><title>Supramolecular organizations in the aerobic respiratory chain of Escherichia coli</title><title>Biochimie</title><addtitle>Biochimie</addtitle><description>The organization of respiratory chain complexes in supercomplexes has been shown in the mitochondria of several eukaryotes and in the cell membranes of some bacteria. These supercomplexes are suggested to be important for oxidative phosphorylation efficiency and to prevent the formation of reactive oxygen species.
Here we describe, for the first time, the identification of supramolecular organizations in the aerobic respiratory chain of Escherichia coli, including a trimer of succinate dehydrogenase. Furthermore, two heterooligomerizations have been shown: one resulting from the association of the NADH:quinone oxidoreductases NDH-1 and NDH-2, and another composed by the cytochrome bo3 quinol:oxygen reductase, cytochrome bd quinol:oxygen reductase and formate dehydrogenase (fdo). These results are supported by blue native-electrophoresis, mass spectrometry and kinetic data of wild type and mutant E . coli strains.
► The E. coli respiratory chain is organized in supercomplexes. ► A formate dehydrogenase:oxygen reductase supercomplex was identified. ► NDH-1 and NDH-2 are associated in a supercomplex.</description><subject>Aerobic respiratory chain</subject><subject>Aerobiosis</subject><subject>Amino Acid Sequence</subject><subject>Bioenergetics</subject><subject>Cell Membrane - enzymology</subject><subject>Cell Membrane - metabolism</subject><subject>Electron Transport</subject><subject>Electrophoresis</subject><subject>Escherichia coli</subject><subject>Escherichia coli K12 - cytology</subject><subject>Escherichia coli K12 - enzymology</subject><subject>Escherichia coli K12 - metabolism</subject><subject>Molecular Sequence Data</subject><subject>NADH:quinone oxidoreductase</subject><subject>Oxygen reductase</subject><subject>Protein Multimerization</subject><subject>Protein Structure, Quaternary</subject><subject>Solubility</subject><subject>Supercomplex</subject><issn>0300-9084</issn><issn>1638-6183</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1PwzAMhiMEYmPwDxDqjVOH0zZtekFC0_iQJiHE7lGaOixT14ykRRq_nowOjnCyZb_2az-EXFKYUqD5zXpaGatWZprAd2kKNDsiY5qnPM4pT4_JGFKAuASejciZ92sAYJCUp2SUUMigYOmYvLz2Wyc3tkHVN9JF1r3J1nzKztjWR6aNuhVGEp2tjIoc-q1xsrNuF6mVDF2ro7lXK3QmXCIjZRtzTk60bDxeHOKELO_ny9ljvHh-eJrdLWLFgHVxlkORUsqTMuU81SzTRbhKas0AdMnzkNaSFayUqMODhaqRcYW0hLpSlUon5HpYu3X2vUffiY3xCptGtmh7LzjnUPIkgf-VjBZZuUc2IdmgVM5671CLrTMb6XaCgthDF2sxQBd76PtqgB7Grg4GfbXB-nfoh3IQ3A4CDDw-DDrhlcFWYW0cqk7U1vzt8AXEA5TE</recordid><startdate>20110301</startdate><enddate>20110301</enddate><creator>Sousa, Pedro M.F.</creator><creator>Silva, Sara T.N.</creator><creator>Hood, Brian L.</creator><creator>Charro, Nuno</creator><creator>Carita, João N.</creator><creator>Vaz, Fátima</creator><creator>Penque, Deborah</creator><creator>Conrads, Thomas P.</creator><creator>Melo, Ana M.P.</creator><general>Elsevier B.V</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>7X8</scope><scope>7QL</scope><scope>C1K</scope></search><sort><creationdate>20110301</creationdate><title>Supramolecular organizations in the aerobic respiratory chain of Escherichia coli</title><author>Sousa, Pedro M.F. ; Silva, Sara T.N. ; Hood, Brian L. ; Charro, Nuno ; Carita, João N. ; Vaz, Fátima ; Penque, Deborah ; Conrads, Thomas P. ; Melo, Ana M.P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c505t-46073118293883f54f7210aff500f9860afda5759aef0107cde58ce190dbcbc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Aerobic respiratory chain</topic><topic>Aerobiosis</topic><topic>Amino Acid Sequence</topic><topic>Bioenergetics</topic><topic>Cell Membrane - enzymology</topic><topic>Cell Membrane - metabolism</topic><topic>Electron Transport</topic><topic>Electrophoresis</topic><topic>Escherichia coli</topic><topic>Escherichia coli K12 - cytology</topic><topic>Escherichia coli K12 - enzymology</topic><topic>Escherichia coli K12 - metabolism</topic><topic>Molecular Sequence Data</topic><topic>NADH:quinone oxidoreductase</topic><topic>Oxygen reductase</topic><topic>Protein Multimerization</topic><topic>Protein Structure, Quaternary</topic><topic>Solubility</topic><topic>Supercomplex</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sousa, Pedro M.F.</creatorcontrib><creatorcontrib>Silva, Sara T.N.</creatorcontrib><creatorcontrib>Hood, Brian L.</creatorcontrib><creatorcontrib>Charro, Nuno</creatorcontrib><creatorcontrib>Carita, João N.</creatorcontrib><creatorcontrib>Vaz, Fátima</creatorcontrib><creatorcontrib>Penque, Deborah</creatorcontrib><creatorcontrib>Conrads, Thomas P.</creatorcontrib><creatorcontrib>Melo, Ana M.P.</creatorcontrib><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><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Biochimie</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sousa, Pedro M.F.</au><au>Silva, Sara T.N.</au><au>Hood, Brian L.</au><au>Charro, Nuno</au><au>Carita, João N.</au><au>Vaz, Fátima</au><au>Penque, Deborah</au><au>Conrads, Thomas P.</au><au>Melo, Ana M.P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Supramolecular organizations in the aerobic respiratory chain of Escherichia coli</atitle><jtitle>Biochimie</jtitle><addtitle>Biochimie</addtitle><date>2011-03-01</date><risdate>2011</risdate><volume>93</volume><issue>3</issue><spage>418</spage><epage>425</epage><pages>418-425</pages><issn>0300-9084</issn><eissn>1638-6183</eissn><abstract>The organization of respiratory chain complexes in supercomplexes has been shown in the mitochondria of several eukaryotes and in the cell membranes of some bacteria. These supercomplexes are suggested to be important for oxidative phosphorylation efficiency and to prevent the formation of reactive oxygen species.
Here we describe, for the first time, the identification of supramolecular organizations in the aerobic respiratory chain of Escherichia coli, including a trimer of succinate dehydrogenase. Furthermore, two heterooligomerizations have been shown: one resulting from the association of the NADH:quinone oxidoreductases NDH-1 and NDH-2, and another composed by the cytochrome bo3 quinol:oxygen reductase, cytochrome bd quinol:oxygen reductase and formate dehydrogenase (fdo). These results are supported by blue native-electrophoresis, mass spectrometry and kinetic data of wild type and mutant E . coli strains.
► The E. coli respiratory chain is organized in supercomplexes. ► A formate dehydrogenase:oxygen reductase supercomplex was identified. ► NDH-1 and NDH-2 are associated in a supercomplex.</abstract><cop>France</cop><pub>Elsevier B.V</pub><pmid>21040753</pmid><doi>10.1016/j.biochi.2010.10.014</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0300-9084 |
| ispartof | Biochimie, 2011-03, Vol.93 (3), p.418-425 |
| issn | 0300-9084 1638-6183 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_888098220 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Aerobic respiratory chain Aerobiosis Amino Acid Sequence Bioenergetics Cell Membrane - enzymology Cell Membrane - metabolism Electron Transport Electrophoresis Escherichia coli Escherichia coli K12 - cytology Escherichia coli K12 - enzymology Escherichia coli K12 - metabolism Molecular Sequence Data NADH:quinone oxidoreductase Oxygen reductase Protein Multimerization Protein Structure, Quaternary Solubility Supercomplex |
| title | Supramolecular organizations in the aerobic respiratory chain of Escherichia coli |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-23T22%3A01%3A21IST&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=Supramolecular%20organizations%20in%20the%20aerobic%20respiratory%20chain%20of%20Escherichia%20coli&rft.jtitle=Biochimie&rft.au=Sousa,%20Pedro%20M.F.&rft.date=2011-03-01&rft.volume=93&rft.issue=3&rft.spage=418&rft.epage=425&rft.pages=418-425&rft.issn=0300-9084&rft.eissn=1638-6183&rft_id=info:doi/10.1016/j.biochi.2010.10.014&rft_dat=%3Cproquest_cross%3E851749618%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=851749618&rft_id=info:pmid/21040753&rft_els_id=S0300908410003743&rfr_iscdi=true |