The [NiFe]-hydrogenase accessory chaperones HypC and HybG of Escherichia coli are iron- and carbon dioxide-binding proteins
•We isolated HypC [NiFe]-hydrogenase accessory proteins with bound Fe and CO2.•Coordination of both Fe and CO2 depends on conserved cysteine and histidine residues.•Binding of both Fe and CO2 is highly oxygen-sensitive.•Binding of Fe and CO2 is independent of the other Hyp accessory proteins. [NiFe]...
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| Veröffentlicht in: | FEBS letters 2013-08, Vol.587 (16), p.2512-2516 |
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| creator | Soboh, Basem Stripp, Sven T. Bielak, Claudia Lindenstrauß, Ute Braussemann, Mario Javaid, Mahwish Hallensleben, Magnus Granich, Claudia Herzberg, Martin Heberle, Joachim Sawers, R. Gary |
| description | •We isolated HypC [NiFe]-hydrogenase accessory proteins with bound Fe and CO2.•Coordination of both Fe and CO2 depends on conserved cysteine and histidine residues.•Binding of both Fe and CO2 is highly oxygen-sensitive.•Binding of Fe and CO2 is independent of the other Hyp accessory proteins.
[NiFe]-hydrogenase accessory proteins HypC and HypD form a complex that binds a Fe–(CN)2CO moiety and CO2. In this study two HypC homologues from Escherichia coli were purified under strictly anaerobic conditions and both contained sub-stoichiometric amounts of iron (approx. 0.3molFe/mol HypC). Infrared spectroscopic analysis identified a signature at 2337cm−1 indicating bound CO2. Aerobically isolated HypC lacked both Fe and CO2. Exchange of either of the highly conserved amino acid residues Cys2 or His51 abolished both Fe- and CO2-binding. Our results suggest that HypC delivers CO2 bound directly to Fe for reduction to CO by HypD.
HypC and HypCbind by comigration in sds page (View interaction)
HybG and HybGbind by comigration in sds page (View interaction) |
| doi_str_mv | 10.1016/j.febslet.2013.06.055 |
| format | Article |
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[NiFe]-hydrogenase accessory proteins HypC and HypD form a complex that binds a Fe–(CN)2CO moiety and CO2. In this study two HypC homologues from Escherichia coli were purified under strictly anaerobic conditions and both contained sub-stoichiometric amounts of iron (approx. 0.3molFe/mol HypC). Infrared spectroscopic analysis identified a signature at 2337cm−1 indicating bound CO2. Aerobically isolated HypC lacked both Fe and CO2. Exchange of either of the highly conserved amino acid residues Cys2 or His51 abolished both Fe- and CO2-binding. Our results suggest that HypC delivers CO2 bound directly to Fe for reduction to CO by HypD.
HypC and HypCbind by comigration in sds page (View interaction)
HybG and HybGbind by comigration in sds page (View interaction)</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2013.06.055</identifier><identifier>PMID: 23851071</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>carbon ; Carbon dioxide ; Carbon Dioxide - chemistry ; Carrier Proteins - chemistry ; Cysteine - chemistry ; Escherichia coli ; Escherichia coli - enzymology ; Escherichia coli Proteins - chemistry ; Histidine - chemistry ; Hydrogen Peroxide - chemistry ; Hydrogenase ; Hydrogenase - chemistry ; Infrared spectroscopy ; Iron ; Iron - chemistry ; Ligands ; Maturation ; Metalloprotein ; Molecular Chaperones - chemistry ; Oxidation-Reduction ; Oxygen - chemistry ; proteins</subject><ispartof>FEBS letters, 2013-08, Vol.587 (16), p.2512-2516</ispartof><rights>2013 Federation of European Biochemical Societies</rights><rights>FEBS Letters 587 (2013) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5436-8821fdd807d28b76125405d02bbe726575bef52bf4ac188de7e7b1bdb41cfd623</citedby><cites>FETCH-LOGICAL-c5436-8821fdd807d28b76125405d02bbe726575bef52bf4ac188de7e7b1bdb41cfd623</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2013.06.055$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.febslet.2013.06.055$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,778,782,1414,1430,3539,27911,27912,45561,45562,45982,46396,46820</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23851071$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Soboh, Basem</creatorcontrib><creatorcontrib>Stripp, Sven T.</creatorcontrib><creatorcontrib>Bielak, Claudia</creatorcontrib><creatorcontrib>Lindenstrauß, Ute</creatorcontrib><creatorcontrib>Braussemann, Mario</creatorcontrib><creatorcontrib>Javaid, Mahwish</creatorcontrib><creatorcontrib>Hallensleben, Magnus</creatorcontrib><creatorcontrib>Granich, Claudia</creatorcontrib><creatorcontrib>Herzberg, Martin</creatorcontrib><creatorcontrib>Heberle, Joachim</creatorcontrib><creatorcontrib>Sawers, R. Gary</creatorcontrib><title>The [NiFe]-hydrogenase accessory chaperones HypC and HybG of Escherichia coli are iron- and carbon dioxide-binding proteins</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>•We isolated HypC [NiFe]-hydrogenase accessory proteins with bound Fe and CO2.•Coordination of both Fe and CO2 depends on conserved cysteine and histidine residues.•Binding of both Fe and CO2 is highly oxygen-sensitive.•Binding of Fe and CO2 is independent of the other Hyp accessory proteins.
[NiFe]-hydrogenase accessory proteins HypC and HypD form a complex that binds a Fe–(CN)2CO moiety and CO2. In this study two HypC homologues from Escherichia coli were purified under strictly anaerobic conditions and both contained sub-stoichiometric amounts of iron (approx. 0.3molFe/mol HypC). Infrared spectroscopic analysis identified a signature at 2337cm−1 indicating bound CO2. Aerobically isolated HypC lacked both Fe and CO2. Exchange of either of the highly conserved amino acid residues Cys2 or His51 abolished both Fe- and CO2-binding. Our results suggest that HypC delivers CO2 bound directly to Fe for reduction to CO by HypD.
HypC and HypCbind by comigration in sds page (View interaction)
HybG and HybGbind by comigration in sds page (View interaction)</description><subject>carbon</subject><subject>Carbon dioxide</subject><subject>Carbon Dioxide - chemistry</subject><subject>Carrier Proteins - chemistry</subject><subject>Cysteine - chemistry</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Histidine - chemistry</subject><subject>Hydrogen Peroxide - chemistry</subject><subject>Hydrogenase</subject><subject>Hydrogenase - chemistry</subject><subject>Infrared spectroscopy</subject><subject>Iron</subject><subject>Iron - chemistry</subject><subject>Ligands</subject><subject>Maturation</subject><subject>Metalloprotein</subject><subject>Molecular Chaperones - chemistry</subject><subject>Oxidation-Reduction</subject><subject>Oxygen - chemistry</subject><subject>proteins</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkk1vEzEQhlcIRNPCTwD5yGUXf6w_ckIQJQ1SBQfKCSHLH7NdR5t1sBNgxZ-vQwLX9jQe6Zl3LD1TVa8Ibggm4u2m6cDmAfYNxYQ1WDSY8yfVjCjJatYK9bSaYUzamss5u6guc97g0isyf15dUKY4wZLMqj-3PaBvn8IKvtf95FO8g9FkQMY5yDmmCbne7CDFETJaT7sFMqMvD3uNYoeW2fWQguuDQS4OAZkEKBS4_os5k2wckQ_xd_BQ2zD6MN6hXYp7CGN-UT3rzJDh5bleVV9Xy9vFur75fP1x8f6mdrxlolaKks57haWnykpBKG8x95haC5IKLrmFjlPbtcYRpTxIkJZYb1viOi8ou6renHLL4h8HyHu9DdnBMJgR4iFrRjiTosVKPYgSweatbLF8BNoWMVxSyQvKT6hLMecEnd6lsDVp0gTro0290Web-mhTY6GLzTL3-rziYLfg_0_901eA9Qn4FQaYHpeqV8sP9MvxNI6XQRjGnEhRot6doqCY-Bkg6ewCjA58SOD22sfwwG_vAYeQyHk</recordid><startdate>20130819</startdate><enddate>20130819</enddate><creator>Soboh, Basem</creator><creator>Stripp, Sven T.</creator><creator>Bielak, Claudia</creator><creator>Lindenstrauß, Ute</creator><creator>Braussemann, Mario</creator><creator>Javaid, Mahwish</creator><creator>Hallensleben, Magnus</creator><creator>Granich, Claudia</creator><creator>Herzberg, Martin</creator><creator>Heberle, Joachim</creator><creator>Sawers, R. Gary</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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><scope>7QL</scope><scope>C1K</scope><scope>7S9</scope><scope>L.6</scope></search><sort><creationdate>20130819</creationdate><title>The [NiFe]-hydrogenase accessory chaperones HypC and HybG of Escherichia coli are iron- and carbon dioxide-binding proteins</title><author>Soboh, Basem ; Stripp, Sven T. ; Bielak, Claudia ; Lindenstrauß, Ute ; Braussemann, Mario ; Javaid, Mahwish ; Hallensleben, Magnus ; Granich, Claudia ; Herzberg, Martin ; Heberle, Joachim ; Sawers, R. Gary</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5436-8821fdd807d28b76125405d02bbe726575bef52bf4ac188de7e7b1bdb41cfd623</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>carbon</topic><topic>Carbon dioxide</topic><topic>Carbon Dioxide - chemistry</topic><topic>Carrier Proteins - chemistry</topic><topic>Cysteine - chemistry</topic><topic>Escherichia coli</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Histidine - chemistry</topic><topic>Hydrogen Peroxide - chemistry</topic><topic>Hydrogenase</topic><topic>Hydrogenase - chemistry</topic><topic>Infrared spectroscopy</topic><topic>Iron</topic><topic>Iron - chemistry</topic><topic>Ligands</topic><topic>Maturation</topic><topic>Metalloprotein</topic><topic>Molecular Chaperones - chemistry</topic><topic>Oxidation-Reduction</topic><topic>Oxygen - chemistry</topic><topic>proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Soboh, Basem</creatorcontrib><creatorcontrib>Stripp, Sven T.</creatorcontrib><creatorcontrib>Bielak, Claudia</creatorcontrib><creatorcontrib>Lindenstrauß, Ute</creatorcontrib><creatorcontrib>Braussemann, Mario</creatorcontrib><creatorcontrib>Javaid, Mahwish</creatorcontrib><creatorcontrib>Hallensleben, Magnus</creatorcontrib><creatorcontrib>Granich, Claudia</creatorcontrib><creatorcontrib>Herzberg, Martin</creatorcontrib><creatorcontrib>Heberle, Joachim</creatorcontrib><creatorcontrib>Sawers, R. Gary</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Soboh, Basem</au><au>Stripp, Sven T.</au><au>Bielak, Claudia</au><au>Lindenstrauß, Ute</au><au>Braussemann, Mario</au><au>Javaid, Mahwish</au><au>Hallensleben, Magnus</au><au>Granich, Claudia</au><au>Herzberg, Martin</au><au>Heberle, Joachim</au><au>Sawers, R. Gary</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The [NiFe]-hydrogenase accessory chaperones HypC and HybG of Escherichia coli are iron- and carbon dioxide-binding proteins</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2013-08-19</date><risdate>2013</risdate><volume>587</volume><issue>16</issue><spage>2512</spage><epage>2516</epage><pages>2512-2516</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>•We isolated HypC [NiFe]-hydrogenase accessory proteins with bound Fe and CO2.•Coordination of both Fe and CO2 depends on conserved cysteine and histidine residues.•Binding of both Fe and CO2 is highly oxygen-sensitive.•Binding of Fe and CO2 is independent of the other Hyp accessory proteins.
[NiFe]-hydrogenase accessory proteins HypC and HypD form a complex that binds a Fe–(CN)2CO moiety and CO2. In this study two HypC homologues from Escherichia coli were purified under strictly anaerobic conditions and both contained sub-stoichiometric amounts of iron (approx. 0.3molFe/mol HypC). Infrared spectroscopic analysis identified a signature at 2337cm−1 indicating bound CO2. Aerobically isolated HypC lacked both Fe and CO2. Exchange of either of the highly conserved amino acid residues Cys2 or His51 abolished both Fe- and CO2-binding. Our results suggest that HypC delivers CO2 bound directly to Fe for reduction to CO by HypD.
HypC and HypCbind by comigration in sds page (View interaction)
HybG and HybGbind by comigration in sds page (View interaction)</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>23851071</pmid><doi>10.1016/j.febslet.2013.06.055</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | carbon Carbon dioxide Carbon Dioxide - chemistry Carrier Proteins - chemistry Cysteine - chemistry Escherichia coli Escherichia coli - enzymology Escherichia coli Proteins - chemistry Histidine - chemistry Hydrogen Peroxide - chemistry Hydrogenase Hydrogenase - chemistry Infrared spectroscopy Iron Iron - chemistry Ligands Maturation Metalloprotein Molecular Chaperones - chemistry Oxidation-Reduction Oxygen - chemistry proteins |
| title | The [NiFe]-hydrogenase accessory chaperones HypC and HybG of Escherichia coli are iron- and carbon dioxide-binding proteins |
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