In the absence of thioredoxins, what are the reductants for peroxiredoxins in Thermotoga maritima?
Three peroxiredoxins (Prxs) were identified in Thermotoga maritima, which possesses neither glutathione nor typical thioredoxins: one of the Prx6 class; one 2-Cys PrxBCP; and a unique hybrid protein containing an N-terminal 1-Cys PrxBCP domain fused to a flavin mononucleotide-containing nitroreducta...
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| Veröffentlicht in: | Antioxidants & redox signaling 2013-05, Vol.18 (13), p.1613-1622 |
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| creator | Couturier, Jérémy Prosper, Pascalita Winger, Alison M Hecker, Arnaud Hirasawa, Masakazu Knaff, David B Gans, Pierre Jacquot, Jean-Pierre Navaza, Alda Haouz, Ahmed Rouhier, Nicolas |
| description | Three peroxiredoxins (Prxs) were identified in Thermotoga maritima, which possesses neither glutathione nor typical thioredoxins: one of the Prx6 class; one 2-Cys PrxBCP; and a unique hybrid protein containing an N-terminal 1-Cys PrxBCP domain fused to a flavin mononucleotide-containing nitroreductase (Ntr) domain. No peroxidase activity was detected for Prx6, whereas both bacterioferritin comigratory proteins (BCPs) were regenerated by a NADH/thioredoxin reductase/glutaredoxin (Grx)-like system, constituting a unique peroxide removal system. Only two of the three Grx-like proteins were able to support peroxidase activity. The inability of TmGrx1 to regenerate oxidized 2-Cys PrxBCP probably results from the thermodynamically unfavorable difference in their disulfide/dithiol E(m) values, -150 and -315 mV, respectively. Mutagenesis of the Prx-Ntr fusion, combined with kinetic and structural analyses, indicated that electrons are not transferred between its two domains. However, their separate activities could function in a complementary manner, with peroxide originating from the chromate reductase activity of the Ntr domain reduced by the Prx domain. |
| doi_str_mv | 10.1089/ars.2012.4739 |
| format | Article |
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No peroxidase activity was detected for Prx6, whereas both bacterioferritin comigratory proteins (BCPs) were regenerated by a NADH/thioredoxin reductase/glutaredoxin (Grx)-like system, constituting a unique peroxide removal system. Only two of the three Grx-like proteins were able to support peroxidase activity. The inability of TmGrx1 to regenerate oxidized 2-Cys PrxBCP probably results from the thermodynamically unfavorable difference in their disulfide/dithiol E(m) values, -150 and -315 mV, respectively. Mutagenesis of the Prx-Ntr fusion, combined with kinetic and structural analyses, indicated that electrons are not transferred between its two domains. However, their separate activities could function in a complementary manner, with peroxide originating from the chromate reductase activity of the Ntr domain reduced by the Prx domain.</description><identifier>ISSN: 1523-0864</identifier><identifier>EISSN: 1557-7716</identifier><identifier>DOI: 10.1089/ars.2012.4739</identifier><identifier>PMID: 22866991</identifier><language>eng</language><publisher>United States: Mary Ann Liebert</publisher><subject>Catalysis ; Forum & Views ; Life Sciences ; Oxidation-Reduction ; Oxidoreductases - metabolism ; Peroxidase - metabolism ; Peroxiredoxins - chemistry ; Peroxiredoxins - metabolism ; Protein Conformation ; Protein Interaction Domains and Motifs ; Protein Multimerization ; Reducing Agents - metabolism ; Thermotoga maritima ; Thermotoga maritima - metabolism ; Thioredoxins - metabolism</subject><ispartof>Antioxidants & redox signaling, 2013-05, Vol.18 (13), p.1613-1622</ispartof><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><rights>Copyright 2013, Mary Ann Liebert, Inc. 2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c454t-cb1adc046977c6d029f2e487d3820c1d8a597b92f53910e09e73777db69703b33</citedby><cites>FETCH-LOGICAL-c454t-cb1adc046977c6d029f2e487d3820c1d8a597b92f53910e09e73777db69703b33</cites><orcidid>0000-0002-2036-7884 ; 0000-0003-3127-2669 ; 0000-0003-4511-5410 ; 0000-0003-4975-8587 ; 0000-0002-0697-6552 ; 0000-0003-1196-1635</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22866991$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-01268123$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Couturier, Jérémy</creatorcontrib><creatorcontrib>Prosper, Pascalita</creatorcontrib><creatorcontrib>Winger, Alison M</creatorcontrib><creatorcontrib>Hecker, Arnaud</creatorcontrib><creatorcontrib>Hirasawa, Masakazu</creatorcontrib><creatorcontrib>Knaff, David B</creatorcontrib><creatorcontrib>Gans, Pierre</creatorcontrib><creatorcontrib>Jacquot, Jean-Pierre</creatorcontrib><creatorcontrib>Navaza, Alda</creatorcontrib><creatorcontrib>Haouz, Ahmed</creatorcontrib><creatorcontrib>Rouhier, Nicolas</creatorcontrib><title>In the absence of thioredoxins, what are the reductants for peroxiredoxins in Thermotoga maritima?</title><title>Antioxidants & redox signaling</title><addtitle>Antioxid Redox Signal</addtitle><description>Three peroxiredoxins (Prxs) were identified in Thermotoga maritima, which possesses neither glutathione nor typical thioredoxins: one of the Prx6 class; one 2-Cys PrxBCP; and a unique hybrid protein containing an N-terminal 1-Cys PrxBCP domain fused to a flavin mononucleotide-containing nitroreductase (Ntr) domain. No peroxidase activity was detected for Prx6, whereas both bacterioferritin comigratory proteins (BCPs) were regenerated by a NADH/thioredoxin reductase/glutaredoxin (Grx)-like system, constituting a unique peroxide removal system. Only two of the three Grx-like proteins were able to support peroxidase activity. The inability of TmGrx1 to regenerate oxidized 2-Cys PrxBCP probably results from the thermodynamically unfavorable difference in their disulfide/dithiol E(m) values, -150 and -315 mV, respectively. Mutagenesis of the Prx-Ntr fusion, combined with kinetic and structural analyses, indicated that electrons are not transferred between its two domains. However, their separate activities could function in a complementary manner, with peroxide originating from the chromate reductase activity of the Ntr domain reduced by the Prx domain.</description><subject>Catalysis</subject><subject>Forum & Views</subject><subject>Life Sciences</subject><subject>Oxidation-Reduction</subject><subject>Oxidoreductases - metabolism</subject><subject>Peroxidase - metabolism</subject><subject>Peroxiredoxins - chemistry</subject><subject>Peroxiredoxins - metabolism</subject><subject>Protein Conformation</subject><subject>Protein Interaction Domains and Motifs</subject><subject>Protein Multimerization</subject><subject>Reducing Agents - metabolism</subject><subject>Thermotoga maritima</subject><subject>Thermotoga maritima - metabolism</subject><subject>Thioredoxins - metabolism</subject><issn>1523-0864</issn><issn>1557-7716</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkUtv1DAURi1E1ZbSJVvkJUhkuLYTPzagqoK20khsytpynJsmaBIPtqfAv8fptFXble3rc48fHyHvGKwYaPPZxbTiwPiqVsK8IsesaVSlFJOvlzkXFWhZH5E3Kf0CAM4YHJIjzrWUxrBj0l7NNA9IXZtw9khDX5ZjiNiFv-OcPtE_g8vURbyjSnnns5tzon2IdIuxUA8sHWd6PWCcQg43jk4ujnmc3Ne35KB3m4Sn9-MJ-fn92_X5ZbX-cXF1fraufN3UufItc52HWhqlvOyAm55jrVUnNAfPOu0ao1rD-0YYBggGlVBKdW1pANEKcUK-7L3bXTth53HO0W3sNpZLxH82uNE-35nHwd6EWyskE0yrIvi4Fwwv2i7P1naplW-WmnFxywr74f6wGH7vMGU7jcnjZuNmDLtkmZSa1wZg0VZ71MeQUsT-0c3ALhnakqFdMrRLhoV___Qdj_RDaOI_A6eYcw</recordid><startdate>20130501</startdate><enddate>20130501</enddate><creator>Couturier, Jérémy</creator><creator>Prosper, Pascalita</creator><creator>Winger, Alison M</creator><creator>Hecker, Arnaud</creator><creator>Hirasawa, Masakazu</creator><creator>Knaff, David B</creator><creator>Gans, Pierre</creator><creator>Jacquot, Jean-Pierre</creator><creator>Navaza, Alda</creator><creator>Haouz, Ahmed</creator><creator>Rouhier, Nicolas</creator><general>Mary Ann Liebert</general><general>Mary Ann Liebert, Inc</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>1XC</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-2036-7884</orcidid><orcidid>https://orcid.org/0000-0003-3127-2669</orcidid><orcidid>https://orcid.org/0000-0003-4511-5410</orcidid><orcidid>https://orcid.org/0000-0003-4975-8587</orcidid><orcidid>https://orcid.org/0000-0002-0697-6552</orcidid><orcidid>https://orcid.org/0000-0003-1196-1635</orcidid></search><sort><creationdate>20130501</creationdate><title>In the absence of thioredoxins, what are the reductants for peroxiredoxins in Thermotoga maritima?</title><author>Couturier, Jérémy ; Prosper, Pascalita ; Winger, Alison M ; Hecker, Arnaud ; Hirasawa, Masakazu ; Knaff, David B ; Gans, Pierre ; Jacquot, Jean-Pierre ; Navaza, Alda ; Haouz, Ahmed ; Rouhier, Nicolas</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c454t-cb1adc046977c6d029f2e487d3820c1d8a597b92f53910e09e73777db69703b33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Catalysis</topic><topic>Forum & Views</topic><topic>Life Sciences</topic><topic>Oxidation-Reduction</topic><topic>Oxidoreductases - metabolism</topic><topic>Peroxidase - metabolism</topic><topic>Peroxiredoxins - chemistry</topic><topic>Peroxiredoxins - metabolism</topic><topic>Protein Conformation</topic><topic>Protein Interaction Domains and Motifs</topic><topic>Protein Multimerization</topic><topic>Reducing Agents - metabolism</topic><topic>Thermotoga maritima</topic><topic>Thermotoga maritima - metabolism</topic><topic>Thioredoxins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Couturier, Jérémy</creatorcontrib><creatorcontrib>Prosper, Pascalita</creatorcontrib><creatorcontrib>Winger, Alison M</creatorcontrib><creatorcontrib>Hecker, Arnaud</creatorcontrib><creatorcontrib>Hirasawa, Masakazu</creatorcontrib><creatorcontrib>Knaff, David B</creatorcontrib><creatorcontrib>Gans, Pierre</creatorcontrib><creatorcontrib>Jacquot, Jean-Pierre</creatorcontrib><creatorcontrib>Navaza, Alda</creatorcontrib><creatorcontrib>Haouz, Ahmed</creatorcontrib><creatorcontrib>Rouhier, Nicolas</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>Hyper Article en Ligne (HAL)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Antioxidants & redox signaling</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Couturier, Jérémy</au><au>Prosper, Pascalita</au><au>Winger, Alison M</au><au>Hecker, Arnaud</au><au>Hirasawa, Masakazu</au><au>Knaff, David B</au><au>Gans, Pierre</au><au>Jacquot, Jean-Pierre</au><au>Navaza, Alda</au><au>Haouz, Ahmed</au><au>Rouhier, Nicolas</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>In the absence of thioredoxins, what are the reductants for peroxiredoxins in Thermotoga maritima?</atitle><jtitle>Antioxidants & redox signaling</jtitle><addtitle>Antioxid Redox Signal</addtitle><date>2013-05-01</date><risdate>2013</risdate><volume>18</volume><issue>13</issue><spage>1613</spage><epage>1622</epage><pages>1613-1622</pages><issn>1523-0864</issn><eissn>1557-7716</eissn><abstract>Three peroxiredoxins (Prxs) were identified in Thermotoga maritima, which possesses neither glutathione nor typical thioredoxins: one of the Prx6 class; one 2-Cys PrxBCP; and a unique hybrid protein containing an N-terminal 1-Cys PrxBCP domain fused to a flavin mononucleotide-containing nitroreductase (Ntr) domain. No peroxidase activity was detected for Prx6, whereas both bacterioferritin comigratory proteins (BCPs) were regenerated by a NADH/thioredoxin reductase/glutaredoxin (Grx)-like system, constituting a unique peroxide removal system. Only two of the three Grx-like proteins were able to support peroxidase activity. The inability of TmGrx1 to regenerate oxidized 2-Cys PrxBCP probably results from the thermodynamically unfavorable difference in their disulfide/dithiol E(m) values, -150 and -315 mV, respectively. Mutagenesis of the Prx-Ntr fusion, combined with kinetic and structural analyses, indicated that electrons are not transferred between its two domains. However, their separate activities could function in a complementary manner, with peroxide originating from the chromate reductase activity of the Ntr domain reduced by the Prx domain.</abstract><cop>United States</cop><pub>Mary Ann Liebert</pub><pmid>22866991</pmid><doi>10.1089/ars.2012.4739</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0002-2036-7884</orcidid><orcidid>https://orcid.org/0000-0003-3127-2669</orcidid><orcidid>https://orcid.org/0000-0003-4511-5410</orcidid><orcidid>https://orcid.org/0000-0003-4975-8587</orcidid><orcidid>https://orcid.org/0000-0002-0697-6552</orcidid><orcidid>https://orcid.org/0000-0003-1196-1635</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | Antioxidants & redox signaling, 2013-05, Vol.18 (13), p.1613-1622 |
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| subjects | Catalysis Forum & Views Life Sciences Oxidation-Reduction Oxidoreductases - metabolism Peroxidase - metabolism Peroxiredoxins - chemistry Peroxiredoxins - metabolism Protein Conformation Protein Interaction Domains and Motifs Protein Multimerization Reducing Agents - metabolism Thermotoga maritima Thermotoga maritima - metabolism Thioredoxins - metabolism |
| title | In the absence of thioredoxins, what are the reductants for peroxiredoxins in Thermotoga maritima? |
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