An Escherichia coli hydrogenase‐3‐type hydrogenase in methanogenic archaea
Methanogenic archaea are known to contain two types of [NiFe] hydrogenases designated F420‐reducing hydrogenase and F420‐non‐reducing hydrogenase. We report here that they additionally contain Escherichia coli hydrogenase‐3‐type [NiFe] hydrogenases. The evidence is based on biochemical studies and a...
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| Veröffentlicht in: | European journal of biochemistry 1998-03, Vol.252 (3), p.467-476 |
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| creator | Künkel, Andreas Vorholt, Julia A. Thauer, Rudolf K. Hedderich, Reiner |
| description | Methanogenic archaea are known to contain two types of [NiFe] hydrogenases designated F420‐reducing hydrogenase and F420‐non‐reducing hydrogenase. We report here that they additionally contain Escherichia coli hydrogenase‐3‐type [NiFe] hydrogenases. The evidence is based on biochemical studies and analysis of the subunit primary structure of this hydrogenase (designated Ech) purified from membranes of acetate‐grown cells of Methanosarcina barkeri. The subunits EchE and EchC of the EchABCDEF complex showed 34 % and 45 % sequence identity to the nickel‐containing large subunit HycE and to the iron‐sulfur cluster containing small subunit HycG, respectively, of the hydrogenase in the formate hydrogen lyase complex from E. coli. Analysis of the totally sequenced genomes of Methanococcus jannaschii and Methanobacterium thermoautotrophicum strain ΔH revealed that these organisms contain similar open reading frames, indicating the presence of an E. coli hydrogenase‐3‐type hydrogenase also in these methanogenic archaea. |
| doi_str_mv | 10.1046/j.1432-1327.1998.2520467.x |
| format | Article |
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We report here that they additionally contain Escherichia coli hydrogenase‐3‐type [NiFe] hydrogenases. The evidence is based on biochemical studies and analysis of the subunit primary structure of this hydrogenase (designated Ech) purified from membranes of acetate‐grown cells of Methanosarcina barkeri. The subunits EchE and EchC of the EchABCDEF complex showed 34 % and 45 % sequence identity to the nickel‐containing large subunit HycE and to the iron‐sulfur cluster containing small subunit HycG, respectively, of the hydrogenase in the formate hydrogen lyase complex from E. coli. Analysis of the totally sequenced genomes of Methanococcus jannaschii and Methanobacterium thermoautotrophicum strain ΔH revealed that these organisms contain similar open reading frames, indicating the presence of an E. coli hydrogenase‐3‐type hydrogenase also in these methanogenic archaea.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1046/j.1432-1327.1998.2520467.x</identifier><identifier>PMID: 9546662</identifier><language>eng</language><publisher>Berlin & Heidelberg: Springer‐Verlag</publisher><subject>Amino Acid Sequence ; Cell Membrane - enzymology ; Conserved Sequence ; energy conservation ; Escherichia coli ; Escherichia coli - enzymology ; Escherichia coli - genetics ; Escherichia coli hydrogenase 3 ; hydrogenase ; Hydrogenase - chemistry ; Hydrogenase - genetics ; Hydrogenase - isolation & purification ; hydrogenase 3 ; Macromolecular Substances ; Methanobacterium - enzymology ; Methanobacterium - genetics ; methanogenic Archaea ; Methanosarcina barkeri ; Methanosarcina barkeri - enzymology ; Methanosarcina barkeri - genetics ; Molecular Sequence Data ; NADH :ubiquinone oxidoreductase ; Operon ; Peptide Fragments - chemistry ; Polymerase Chain Reaction ; Protein Structure, Secondary ; Sequence Alignment ; Sequence Homology, Amino Acid ; Species Specificity</subject><ispartof>European journal of biochemistry, 1998-03, Vol.252 (3), p.467-476</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5237-be090b299d019bdc3ee5702436518467b45d48b255f234d57d7d1a5698f89ae3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1046%2Fj.1432-1327.1998.2520467.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1046%2Fj.1432-1327.1998.2520467.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27903,27904,45553,45554</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9546662$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Künkel, Andreas</creatorcontrib><creatorcontrib>Vorholt, Julia A.</creatorcontrib><creatorcontrib>Thauer, Rudolf K.</creatorcontrib><creatorcontrib>Hedderich, Reiner</creatorcontrib><title>An Escherichia coli hydrogenase‐3‐type hydrogenase in methanogenic archaea</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>Methanogenic archaea are known to contain two types of [NiFe] hydrogenases designated F420‐reducing hydrogenase and F420‐non‐reducing hydrogenase. We report here that they additionally contain Escherichia coli hydrogenase‐3‐type [NiFe] hydrogenases. The evidence is based on biochemical studies and analysis of the subunit primary structure of this hydrogenase (designated Ech) purified from membranes of acetate‐grown cells of Methanosarcina barkeri. The subunits EchE and EchC of the EchABCDEF complex showed 34 % and 45 % sequence identity to the nickel‐containing large subunit HycE and to the iron‐sulfur cluster containing small subunit HycG, respectively, of the hydrogenase in the formate hydrogen lyase complex from E. coli. Analysis of the totally sequenced genomes of Methanococcus jannaschii and Methanobacterium thermoautotrophicum strain ΔH revealed that these organisms contain similar open reading frames, indicating the presence of an E. coli hydrogenase‐3‐type hydrogenase also in these methanogenic archaea.</description><subject>Amino Acid Sequence</subject><subject>Cell Membrane - enzymology</subject><subject>Conserved Sequence</subject><subject>energy conservation</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli hydrogenase 3</subject><subject>hydrogenase</subject><subject>Hydrogenase - chemistry</subject><subject>Hydrogenase - genetics</subject><subject>Hydrogenase - isolation & purification</subject><subject>hydrogenase 3</subject><subject>Macromolecular Substances</subject><subject>Methanobacterium - enzymology</subject><subject>Methanobacterium - genetics</subject><subject>methanogenic Archaea</subject><subject>Methanosarcina barkeri</subject><subject>Methanosarcina barkeri - enzymology</subject><subject>Methanosarcina barkeri - genetics</subject><subject>Molecular Sequence Data</subject><subject>NADH :ubiquinone oxidoreductase</subject><subject>Operon</subject><subject>Peptide Fragments - chemistry</subject><subject>Polymerase Chain Reaction</subject><subject>Protein Structure, Secondary</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Species Specificity</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkM9Kw0AQxhdRaq0-ghA8eEvc_5v1VkurQtGDvS-bzdSkpEnNttjefASf0ScxIUG8iYdl2O_7Zob5IXRFcEQwlzeriHBGQ8KoiojWcUQFbXQV7Y_QsLMwY8doiDHhIdVCnqIz71cYY6mlGqCBFlxKSYfoaVwGU-8yqHOX5TZwVZEH2SGtq1corYevj0_WvO1hA7_lIC-DNWwzW7ZC7gJbu8yCPUcnS1t4uOjrCC1m08XkIZw_3z9OxvPQCcpUmADWOKFap5joJHUMQChMOZOCxM0hCRcpjxMqxJIyngqVqpRYIXW8jLUFNkLX3dhNXb3twG_NOvcOisKWUO28UVrFMZHizyBRnDQkeBO87YKurryvYWk2db629cEQbFroZmVasqaFblropodu9k3zZb9ll6wh_WntKTf-pPPf8wIO_5hsZtO7l_7HvgFFsJLU</recordid><startdate>19980315</startdate><enddate>19980315</enddate><creator>Künkel, Andreas</creator><creator>Vorholt, Julia A.</creator><creator>Thauer, Rudolf K.</creator><creator>Hedderich, Reiner</creator><general>Springer‐Verlag</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>C1K</scope><scope>7X8</scope></search><sort><creationdate>19980315</creationdate><title>An Escherichia coli hydrogenase‐3‐type hydrogenase in methanogenic archaea</title><author>Künkel, Andreas ; Vorholt, Julia A. ; Thauer, Rudolf K. ; Hedderich, Reiner</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5237-be090b299d019bdc3ee5702436518467b45d48b255f234d57d7d1a5698f89ae3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Amino Acid Sequence</topic><topic>Cell Membrane - enzymology</topic><topic>Conserved Sequence</topic><topic>energy conservation</topic><topic>Escherichia coli</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli hydrogenase 3</topic><topic>hydrogenase</topic><topic>Hydrogenase - chemistry</topic><topic>Hydrogenase - genetics</topic><topic>Hydrogenase - isolation & purification</topic><topic>hydrogenase 3</topic><topic>Macromolecular Substances</topic><topic>Methanobacterium - enzymology</topic><topic>Methanobacterium - genetics</topic><topic>methanogenic Archaea</topic><topic>Methanosarcina barkeri</topic><topic>Methanosarcina barkeri - enzymology</topic><topic>Methanosarcina barkeri - genetics</topic><topic>Molecular Sequence Data</topic><topic>NADH :ubiquinone oxidoreductase</topic><topic>Operon</topic><topic>Peptide Fragments - chemistry</topic><topic>Polymerase Chain Reaction</topic><topic>Protein Structure, Secondary</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>Species Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Künkel, Andreas</creatorcontrib><creatorcontrib>Vorholt, Julia A.</creatorcontrib><creatorcontrib>Thauer, Rudolf K.</creatorcontrib><creatorcontrib>Hedderich, Reiner</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Künkel, Andreas</au><au>Vorholt, Julia A.</au><au>Thauer, Rudolf K.</au><au>Hedderich, Reiner</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>An Escherichia coli hydrogenase‐3‐type hydrogenase in methanogenic archaea</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1998-03-15</date><risdate>1998</risdate><volume>252</volume><issue>3</issue><spage>467</spage><epage>476</epage><pages>467-476</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>Methanogenic archaea are known to contain two types of [NiFe] hydrogenases designated F420‐reducing hydrogenase and F420‐non‐reducing hydrogenase. We report here that they additionally contain Escherichia coli hydrogenase‐3‐type [NiFe] hydrogenases. The evidence is based on biochemical studies and analysis of the subunit primary structure of this hydrogenase (designated Ech) purified from membranes of acetate‐grown cells of Methanosarcina barkeri. The subunits EchE and EchC of the EchABCDEF complex showed 34 % and 45 % sequence identity to the nickel‐containing large subunit HycE and to the iron‐sulfur cluster containing small subunit HycG, respectively, of the hydrogenase in the formate hydrogen lyase complex from E. coli. Analysis of the totally sequenced genomes of Methanococcus jannaschii and Methanobacterium thermoautotrophicum strain ΔH revealed that these organisms contain similar open reading frames, indicating the presence of an E. coli hydrogenase‐3‐type hydrogenase also in these methanogenic archaea.</abstract><cop>Berlin & Heidelberg</cop><pub>Springer‐Verlag</pub><pmid>9546662</pmid><doi>10.1046/j.1432-1327.1998.2520467.x</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Cell Membrane - enzymology Conserved Sequence energy conservation Escherichia coli Escherichia coli - enzymology Escherichia coli - genetics Escherichia coli hydrogenase 3 hydrogenase Hydrogenase - chemistry Hydrogenase - genetics Hydrogenase - isolation & purification hydrogenase 3 Macromolecular Substances Methanobacterium - enzymology Methanobacterium - genetics methanogenic Archaea Methanosarcina barkeri Methanosarcina barkeri - enzymology Methanosarcina barkeri - genetics Molecular Sequence Data NADH :ubiquinone oxidoreductase Operon Peptide Fragments - chemistry Polymerase Chain Reaction Protein Structure, Secondary Sequence Alignment Sequence Homology, Amino Acid Species Specificity |
| title | An Escherichia coli hydrogenase‐3‐type hydrogenase in methanogenic archaea |
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