Loading…

Properties of a thermostable 4Fe‐ferredoxin from the hyperthermophilic bacterium Thermotoga maritima

A ferredoxin has been purified from one of the most ancient and the most thermophilic bacteria known, Thermotoga maritima, which grous up to 90°C. The reduced protein (Mr approx. 6300) contains a single S = 1 2 [4Fe 4S]1+ cluster with complete cysteinyl ligation, and was unaffected after incubation...

Full description

Saved in:
Bibliographic Details
Published in:FEMS microbiology letters 1994-08, Vol.121 (2), p.165-169
Main Authors: Blamey, Jenny M., Mukund, Swarnalatha, Adams, Michael W.W.
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-c4295-89667ce9769cc27de8591d3fa1425ddb6f9b72f993ea47670f02ebfdf8de585c3
cites cdi_FETCH-LOGICAL-c4295-89667ce9769cc27de8591d3fa1425ddb6f9b72f993ea47670f02ebfdf8de585c3
container_end_page 169
container_issue 2
container_start_page 165
container_title FEMS microbiology letters
container_volume 121
creator Blamey, Jenny M.
Mukund, Swarnalatha
Adams, Michael W.W.
description A ferredoxin has been purified from one of the most ancient and the most thermophilic bacteria known, Thermotoga maritima, which grous up to 90°C. The reduced protein (Mr approx. 6300) contains a single S = 1 2 [4Fe 4S]1+ cluster with complete cysteinyl ligation, and was unaffected after incubation at 95°C for 12 h. It functioned as an electron carrier for T. maritima pyruvate oxidoreductase. Remarkably, the properties and amino acid sequence of this hyperthermophilic bacterial protein are much more similar to those of ferredoxins from hyperthermophilic archaea, rather than ferredoxins from mesophilic and moderately thermophilic bacteria.
doi_str_mv 10.1111/j.1574-6968.1994.tb07094.x
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_76744977</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>76744977</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4295-89667ce9769cc27de8591d3fa1425ddb6f9b72f993ea47670f02ebfdf8de585c3</originalsourceid><addsrcrecordid>eNqVkcFqGzEQhkVJSZ20j1AQpeS2rqTVSqscCsHEScElOaRnodWOapldy5HWxL7lEfKMeZLuxouvJXMZ0P_9GukfhL5RMqV9_VhNaSF5JpQop1QpPu0qIknfdx_Q5CidoAnJZZlRouQndJbSihDCGRGn6FQqJvqaIHcfwwZi5yHh4LDB3RJiG1JnqgYwn8Pr84uDGKEOO7_GLoZ2QPByP7je2M3SN97iytgOot-2-OHtuAt_DW5N9J1vzWf00ZkmwZexn6M_8-uH2W22uLv5NbtaZJYzVWSlEkJaUFIoa5msoSwUrXNnKGdFXVfCqUoyp1QOhkshiSMMKle7soaiLGx-ji4O925ieNxC6nTrk4WmMWsI26R7D-dKyv-CVAjCSsZ78PIA2hhSiuD0JvYfintNiR62oVd6iFwPkethG3rcht715q_jlG3VQn20jvH3-vdRN8maxkWztj4dMc5yWuYD9vOAPfkG9u94gJ7_XlBR5P8AoDiqOw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>16602824</pqid></control><display><type>article</type><title>Properties of a thermostable 4Fe‐ferredoxin from the hyperthermophilic bacterium Thermotoga maritima</title><source>Alma/SFX Local Collection</source><creator>Blamey, Jenny M. ; Mukund, Swarnalatha ; Adams, Michael W.W.</creator><creatorcontrib>Blamey, Jenny M. ; Mukund, Swarnalatha ; Adams, Michael W.W.</creatorcontrib><description>A ferredoxin has been purified from one of the most ancient and the most thermophilic bacteria known, Thermotoga maritima, which grous up to 90°C. The reduced protein (Mr approx. 6300) contains a single S = 1 2 [4Fe 4S]1+ cluster with complete cysteinyl ligation, and was unaffected after incubation at 95°C for 12 h. It functioned as an electron carrier for T. maritima pyruvate oxidoreductase. Remarkably, the properties and amino acid sequence of this hyperthermophilic bacterial protein are much more similar to those of ferredoxins from hyperthermophilic archaea, rather than ferredoxins from mesophilic and moderately thermophilic bacteria.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.1994.tb07094.x</identifier><identifier>PMID: 7926666</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Amino Acid Sequence ; Bacteriology ; Biological and medical sciences ; Evolution ; Fermentation ; Ferredoxins - chemistry ; Ferredoxins - isolation &amp; purification ; Fundamental and applied biological sciences. Psychology ; Gram-Negative Anaerobic Bacteria - chemistry ; Hyperthermophilic Archaea ; Metabolism. Enzymes ; Microbiology ; Molecular Sequence Data ; Thermostability ; Thermotoga maritima</subject><ispartof>FEMS microbiology letters, 1994-08, Vol.121 (2), p.165-169</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4295-89667ce9769cc27de8591d3fa1425ddb6f9b72f993ea47670f02ebfdf8de585c3</citedby><cites>FETCH-LOGICAL-c4295-89667ce9769cc27de8591d3fa1425ddb6f9b72f993ea47670f02ebfdf8de585c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27922,27923</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=4231836$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7926666$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Blamey, Jenny M.</creatorcontrib><creatorcontrib>Mukund, Swarnalatha</creatorcontrib><creatorcontrib>Adams, Michael W.W.</creatorcontrib><title>Properties of a thermostable 4Fe‐ferredoxin from the hyperthermophilic bacterium Thermotoga maritima</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>A ferredoxin has been purified from one of the most ancient and the most thermophilic bacteria known, Thermotoga maritima, which grous up to 90°C. The reduced protein (Mr approx. 6300) contains a single S = 1 2 [4Fe 4S]1+ cluster with complete cysteinyl ligation, and was unaffected after incubation at 95°C for 12 h. It functioned as an electron carrier for T. maritima pyruvate oxidoreductase. Remarkably, the properties and amino acid sequence of this hyperthermophilic bacterial protein are much more similar to those of ferredoxins from hyperthermophilic archaea, rather than ferredoxins from mesophilic and moderately thermophilic bacteria.</description><subject>Amino Acid Sequence</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Evolution</subject><subject>Fermentation</subject><subject>Ferredoxins - chemistry</subject><subject>Ferredoxins - isolation &amp; purification</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gram-Negative Anaerobic Bacteria - chemistry</subject><subject>Hyperthermophilic Archaea</subject><subject>Metabolism. Enzymes</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Thermostability</subject><subject>Thermotoga maritima</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><recordid>eNqVkcFqGzEQhkVJSZ20j1AQpeS2rqTVSqscCsHEScElOaRnodWOapldy5HWxL7lEfKMeZLuxouvJXMZ0P_9GukfhL5RMqV9_VhNaSF5JpQop1QpPu0qIknfdx_Q5CidoAnJZZlRouQndJbSihDCGRGn6FQqJvqaIHcfwwZi5yHh4LDB3RJiG1JnqgYwn8Pr84uDGKEOO7_GLoZ2QPByP7je2M3SN97iytgOot-2-OHtuAt_DW5N9J1vzWf00ZkmwZexn6M_8-uH2W22uLv5NbtaZJYzVWSlEkJaUFIoa5msoSwUrXNnKGdFXVfCqUoyp1QOhkshiSMMKle7soaiLGx-ji4O925ieNxC6nTrk4WmMWsI26R7D-dKyv-CVAjCSsZ78PIA2hhSiuD0JvYfintNiR62oVd6iFwPkethG3rcht715q_jlG3VQn20jvH3-vdRN8maxkWztj4dMc5yWuYD9vOAPfkG9u94gJ7_XlBR5P8AoDiqOw</recordid><startdate>19940815</startdate><enddate>19940815</enddate><creator>Blamey, Jenny M.</creator><creator>Mukund, Swarnalatha</creator><creator>Adams, Michael W.W.</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><scope>IQODW</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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>H99</scope><scope>L.F</scope><scope>L.G</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19940815</creationdate><title>Properties of a thermostable 4Fe‐ferredoxin from the hyperthermophilic bacterium Thermotoga maritima</title><author>Blamey, Jenny M. ; Mukund, Swarnalatha ; Adams, Michael W.W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4295-89667ce9769cc27de8591d3fa1425ddb6f9b72f993ea47670f02ebfdf8de585c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Evolution</topic><topic>Fermentation</topic><topic>Ferredoxins - chemistry</topic><topic>Ferredoxins - isolation &amp; purification</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gram-Negative Anaerobic Bacteria - chemistry</topic><topic>Hyperthermophilic Archaea</topic><topic>Metabolism. Enzymes</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Thermostability</topic><topic>Thermotoga maritima</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Blamey, Jenny M.</creatorcontrib><creatorcontrib>Mukund, Swarnalatha</creatorcontrib><creatorcontrib>Adams, Michael W.W.</creatorcontrib><collection>Pascal-Francis</collection><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>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Aquatic Science &amp; Fisheries Abstracts (ASFA) 1: Biological Sciences &amp; Living Resources</collection><collection>ASFA: Marine Biotechnology Abstracts</collection><collection>Aquatic Science &amp; Fisheries Abstracts (ASFA) Marine Biotechnology Abstracts</collection><collection>Aquatic Science &amp; Fisheries Abstracts (ASFA) Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Blamey, Jenny M.</au><au>Mukund, Swarnalatha</au><au>Adams, Michael W.W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Properties of a thermostable 4Fe‐ferredoxin from the hyperthermophilic bacterium Thermotoga maritima</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>1994-08-15</date><risdate>1994</risdate><volume>121</volume><issue>2</issue><spage>165</spage><epage>169</epage><pages>165-169</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><abstract>A ferredoxin has been purified from one of the most ancient and the most thermophilic bacteria known, Thermotoga maritima, which grous up to 90°C. The reduced protein (Mr approx. 6300) contains a single S = 1 2 [4Fe 4S]1+ cluster with complete cysteinyl ligation, and was unaffected after incubation at 95°C for 12 h. It functioned as an electron carrier for T. maritima pyruvate oxidoreductase. Remarkably, the properties and amino acid sequence of this hyperthermophilic bacterial protein are much more similar to those of ferredoxins from hyperthermophilic archaea, rather than ferredoxins from mesophilic and moderately thermophilic bacteria.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>7926666</pmid><doi>10.1111/j.1574-6968.1994.tb07094.x</doi><tpages>5</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0378-1097
ispartof FEMS microbiology letters, 1994-08, Vol.121 (2), p.165-169
issn 0378-1097
1574-6968
language eng
recordid cdi_proquest_miscellaneous_76744977
source Alma/SFX Local Collection
subjects Amino Acid Sequence
Bacteriology
Biological and medical sciences
Evolution
Fermentation
Ferredoxins - chemistry
Ferredoxins - isolation & purification
Fundamental and applied biological sciences. Psychology
Gram-Negative Anaerobic Bacteria - chemistry
Hyperthermophilic Archaea
Metabolism. Enzymes
Microbiology
Molecular Sequence Data
Thermostability
Thermotoga maritima
title Properties of a thermostable 4Fe‐ferredoxin from the hyperthermophilic bacterium Thermotoga maritima
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-09T17%3A05%3A47IST&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=Properties%20of%20a%20thermostable%204Fe%E2%80%90ferredoxin%20from%20the%20hyperthermophilic%20bacterium%20Thermotoga%20maritima&rft.jtitle=FEMS%20microbiology%20letters&rft.au=Blamey,%20Jenny%20M.&rft.date=1994-08-15&rft.volume=121&rft.issue=2&rft.spage=165&rft.epage=169&rft.pages=165-169&rft.issn=0378-1097&rft.eissn=1574-6968&rft.coden=FMLED7&rft_id=info:doi/10.1111/j.1574-6968.1994.tb07094.x&rft_dat=%3Cproquest_cross%3E76744977%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c4295-89667ce9769cc27de8591d3fa1425ddb6f9b72f993ea47670f02ebfdf8de585c3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=16602824&rft_id=info:pmid/7926666&rfr_iscdi=true