Loading…
Unraveling the Structure and Mechanism of Acetyl-Coenzyme A Synthase
The bifunctional enzyme carbon monoxide dehydrogenase/acetyl-coenzyme A (CoA) synthase (CODH/ACS) is a key enzyme in the Wood−Ljungdahl pathway of carbon fixation. Carbon monoxide is combined with a methyl group and ultimately converted to acetyl-CoA at a unique Ni-containing bimetallic site in the...
Saved in:
| Published in: | Accounts of chemical research 2004-10, Vol.37 (10), p.775-783 |
|---|---|
| Main Author: | |
| Format: | Article |
| Language: | English |
| Subjects: | |
| Citations: | Items that this one cites Items that cite this one |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| cited_by | cdi_FETCH-LOGICAL-a415t-837d07e90bc1d9d88e3697f5c67822f4371938ab3ff40f4e5a30e353c1dba4d93 |
|---|---|
| cites | cdi_FETCH-LOGICAL-a415t-837d07e90bc1d9d88e3697f5c67822f4371938ab3ff40f4e5a30e353c1dba4d93 |
| container_end_page | 783 |
| container_issue | 10 |
| container_start_page | 775 |
| container_title | Accounts of chemical research |
| container_volume | 37 |
| creator | Hegg, Eric L |
| description | The bifunctional enzyme carbon monoxide dehydrogenase/acetyl-coenzyme A (CoA) synthase (CODH/ACS) is a key enzyme in the Wood−Ljungdahl pathway of carbon fixation. Carbon monoxide is combined with a methyl group and ultimately converted to acetyl-CoA at a unique Ni-containing bimetallic site in the A-cluster of this enzyme. Despite years of extensive biochemical and spectroscopic studies and the recent report of three separate crystal structures, the mechanism by which acetyl-CoA is synthesized is still unknown. Over the past two years there have been a number of significant developments regarding ACS. This Account critically examines these recent developments and especially focuses on those areas that are still a matter of debate. |
| doi_str_mv | 10.1021/ar040002e |
| format | article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_66985754</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>66985754</sourcerecordid><originalsourceid>FETCH-LOGICAL-a415t-837d07e90bc1d9d88e3697f5c67822f4371938ab3ff40f4e5a30e353c1dba4d93</originalsourceid><addsrcrecordid>eNpt0E1PwzAMBuAIgdgYHPgDqBeQOBSSJmna49j43gBp2zlKW5d1tOlIWkT59XTqNC6cbNmPbOlF6JTgK4I9cq0MZhhjD_ZQn3APuywIg33Ub2ek7ZnXQ0fWrjaE-eIQ9QhnISEe66PxQhv1BXmm351qCc6sMnVc1QYcpRNnCvFS6cwWTpk6wxiqJndHJeifpgBn6MwaXS2VhWN0kKrcwsm2DtDi7nY-enAnr_ePo-HEVYzwyg2oSLCAEEcxScIkCID6oUh57IvA81JGBQlpoCKapgynDLiiGCinrY4US0I6QBfd3bUpP2uwlSwyG0OeKw1lbaXvhwEXnLXwsoOxKa01kMq1yQplGkmw3EQmd5G19mx7tI4KSP7kNqMWuB3IbAXfu70yH9IXVHA5f5vJp5fpzfN0PJek9eedV7GVq7I2us3kn8e_pdCAhw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>66985754</pqid></control><display><type>article</type><title>Unraveling the Structure and Mechanism of Acetyl-Coenzyme A Synthase</title><source>American Chemical Society:Jisc Collections:American Chemical Society Read & Publish Agreement 2022-2024 (Reading list)</source><creator>Hegg, Eric L</creator><creatorcontrib>Hegg, Eric L</creatorcontrib><description>The bifunctional enzyme carbon monoxide dehydrogenase/acetyl-coenzyme A (CoA) synthase (CODH/ACS) is a key enzyme in the Wood−Ljungdahl pathway of carbon fixation. Carbon monoxide is combined with a methyl group and ultimately converted to acetyl-CoA at a unique Ni-containing bimetallic site in the A-cluster of this enzyme. Despite years of extensive biochemical and spectroscopic studies and the recent report of three separate crystal structures, the mechanism by which acetyl-CoA is synthesized is still unknown. Over the past two years there have been a number of significant developments regarding ACS. This Account critically examines these recent developments and especially focuses on those areas that are still a matter of debate.</description><identifier>ISSN: 0001-4842</identifier><identifier>EISSN: 1520-4898</identifier><identifier>DOI: 10.1021/ar040002e</identifier><identifier>PMID: 15491124</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Acetate-CoA Ligase - chemistry ; Acetate-CoA Ligase - metabolism ; Models, Molecular ; Molecular Structure</subject><ispartof>Accounts of chemical research, 2004-10, Vol.37 (10), p.775-783</ispartof><rights>Copyright © 2004 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a415t-837d07e90bc1d9d88e3697f5c67822f4371938ab3ff40f4e5a30e353c1dba4d93</citedby><cites>FETCH-LOGICAL-a415t-837d07e90bc1d9d88e3697f5c67822f4371938ab3ff40f4e5a30e353c1dba4d93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15491124$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hegg, Eric L</creatorcontrib><title>Unraveling the Structure and Mechanism of Acetyl-Coenzyme A Synthase</title><title>Accounts of chemical research</title><addtitle>Acc. Chem. Res</addtitle><description>The bifunctional enzyme carbon monoxide dehydrogenase/acetyl-coenzyme A (CoA) synthase (CODH/ACS) is a key enzyme in the Wood−Ljungdahl pathway of carbon fixation. Carbon monoxide is combined with a methyl group and ultimately converted to acetyl-CoA at a unique Ni-containing bimetallic site in the A-cluster of this enzyme. Despite years of extensive biochemical and spectroscopic studies and the recent report of three separate crystal structures, the mechanism by which acetyl-CoA is synthesized is still unknown. Over the past two years there have been a number of significant developments regarding ACS. This Account critically examines these recent developments and especially focuses on those areas that are still a matter of debate.</description><subject>Acetate-CoA Ligase - chemistry</subject><subject>Acetate-CoA Ligase - metabolism</subject><subject>Models, Molecular</subject><subject>Molecular Structure</subject><issn>0001-4842</issn><issn>1520-4898</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><recordid>eNpt0E1PwzAMBuAIgdgYHPgDqBeQOBSSJmna49j43gBp2zlKW5d1tOlIWkT59XTqNC6cbNmPbOlF6JTgK4I9cq0MZhhjD_ZQn3APuywIg33Ub2ek7ZnXQ0fWrjaE-eIQ9QhnISEe66PxQhv1BXmm351qCc6sMnVc1QYcpRNnCvFS6cwWTpk6wxiqJndHJeifpgBn6MwaXS2VhWN0kKrcwsm2DtDi7nY-enAnr_ePo-HEVYzwyg2oSLCAEEcxScIkCID6oUh57IvA81JGBQlpoCKapgynDLiiGCinrY4US0I6QBfd3bUpP2uwlSwyG0OeKw1lbaXvhwEXnLXwsoOxKa01kMq1yQplGkmw3EQmd5G19mx7tI4KSP7kNqMWuB3IbAXfu70yH9IXVHA5f5vJp5fpzfN0PJek9eedV7GVq7I2us3kn8e_pdCAhw</recordid><startdate>20041001</startdate><enddate>20041001</enddate><creator>Hegg, Eric L</creator><general>American Chemical Society</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>7X8</scope></search><sort><creationdate>20041001</creationdate><title>Unraveling the Structure and Mechanism of Acetyl-Coenzyme A Synthase</title><author>Hegg, Eric L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a415t-837d07e90bc1d9d88e3697f5c67822f4371938ab3ff40f4e5a30e353c1dba4d93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Acetate-CoA Ligase - chemistry</topic><topic>Acetate-CoA Ligase - metabolism</topic><topic>Models, Molecular</topic><topic>Molecular Structure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hegg, Eric L</creatorcontrib><collection>Istex</collection><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><jtitle>Accounts of chemical research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hegg, Eric L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Unraveling the Structure and Mechanism of Acetyl-Coenzyme A Synthase</atitle><jtitle>Accounts of chemical research</jtitle><addtitle>Acc. Chem. Res</addtitle><date>2004-10-01</date><risdate>2004</risdate><volume>37</volume><issue>10</issue><spage>775</spage><epage>783</epage><pages>775-783</pages><issn>0001-4842</issn><eissn>1520-4898</eissn><abstract>The bifunctional enzyme carbon monoxide dehydrogenase/acetyl-coenzyme A (CoA) synthase (CODH/ACS) is a key enzyme in the Wood−Ljungdahl pathway of carbon fixation. Carbon monoxide is combined with a methyl group and ultimately converted to acetyl-CoA at a unique Ni-containing bimetallic site in the A-cluster of this enzyme. Despite years of extensive biochemical and spectroscopic studies and the recent report of three separate crystal structures, the mechanism by which acetyl-CoA is synthesized is still unknown. Over the past two years there have been a number of significant developments regarding ACS. This Account critically examines these recent developments and especially focuses on those areas that are still a matter of debate.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>15491124</pmid><doi>10.1021/ar040002e</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0001-4842 |
| ispartof | Accounts of chemical research, 2004-10, Vol.37 (10), p.775-783 |
| issn | 0001-4842 1520-4898 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_66985754 |
| source | American Chemical Society:Jisc Collections:American Chemical Society Read & Publish Agreement 2022-2024 (Reading list) |
| subjects | Acetate-CoA Ligase - chemistry Acetate-CoA Ligase - metabolism Models, Molecular Molecular Structure |
| title | Unraveling the Structure and Mechanism of Acetyl-Coenzyme A Synthase |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-27T18%3A15%3A18IST&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=Unraveling%20the%20Structure%20and%20Mechanism%20of%20Acetyl-Coenzyme%20A%20Synthase&rft.jtitle=Accounts%20of%20chemical%20research&rft.au=Hegg,%20Eric%20L&rft.date=2004-10-01&rft.volume=37&rft.issue=10&rft.spage=775&rft.epage=783&rft.pages=775-783&rft.issn=0001-4842&rft.eissn=1520-4898&rft_id=info:doi/10.1021/ar040002e&rft_dat=%3Cproquest_cross%3E66985754%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-a415t-837d07e90bc1d9d88e3697f5c67822f4371938ab3ff40f4e5a30e353c1dba4d93%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=66985754&rft_id=info:pmid/15491124&rfr_iscdi=true |