class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant

Significance Ribonucleotide reductases (RNRs) catalyze nucleotide reduction via complex radical chemistry, providing deoxynucleotides for DNA synthesis in all domains of life. Many anaerobic bacteria and archaea contain the class III O ₂-sensitive RNR, and those that have been studied to date couple...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 2014-09, Vol.111 (36), p.E3756-E3765
Hauptverfasser: Wei, Yifeng, Funk, Michael A, Rosado, Leonardo A, Baek, Jiyeon, Drennan, Catherine L, Stubbe, JoAnne
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page E3765
container_issue 36
container_start_page E3756
container_title Proceedings of the National Academy of Sciences - PNAS
container_volume 111
creator Wei, Yifeng
Funk, Michael A
Rosado, Leonardo A
Baek, Jiyeon
Drennan, Catherine L
Stubbe, JoAnne
description Significance Ribonucleotide reductases (RNRs) catalyze nucleotide reduction via complex radical chemistry, providing deoxynucleotides for DNA synthesis in all domains of life. Many anaerobic bacteria and archaea contain the class III O ₂-sensitive RNR, and those that have been studied to date couple nucleotide reduction to formate oxidation. Here we report the characterization of a second class III RNR subtype that couples nucleotide reduction to the oxidation of thioredoxin. Because of the central role of formate and thiols in many anaerobic processes, the distribution of class III RNRs among different organisms may shed light on aspects of anaerobic biochemistry.
doi_str_mv 10.1073/pnas.1414396111
format Article
fullrecord <record><control><sourceid>proquest_pnas_</sourceid><recordid>TN_cdi_pnas_primary_111_36_E3756</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1803084600</sourcerecordid><originalsourceid>FETCH-LOGICAL-c536t-c1093b105cc899254b29ae2c336babc4e531391126bf171dfff3750cdcf159d83</originalsourceid><addsrcrecordid>eNqNkr1vFDEQxS0EIkegpgNLNDSbeNYfu26QoijASREUkNryeu3Ekc8-7F0E-evj1V2OjwYsWS78mzczTw-hl0BOgHT0dBt1OQEGjEoBAI_QCoiERjBJHqMVIW3X9KxlR-hZKbeEEMl78hQdtRx4B5ytkDNBl4LX6zXOfkhxNsGmyY8WZzvOZtLFYpfTBn-yvhSbvcaDNj4E71Le-IKNjniefPB3Fk83PtWy9MNHrAvWDxpxeo6eOB2KfbF_j9HV-4uv5x-by88f1udnl43hVEyNqdPTAQg3ppey5WxopbatoVQMejDMcgpUArRicNDB6JyjHSdmNA64HHt6jN7tdLfzsLGjsXHKOqht9hudf6qkvfrzJ_obdZ2-q2qSkIJXgbd7gZy-zbZMqi5pbAg62jQXBT2hpGeCkH-jXIieLlb_Dwq1fy9ERd_8hd6mOcdq2kJRWY-glTrdUSanUrJ1hxWBqCUZakmG-pWMWvHqd2cO_EMUKoD3wFJ5kANQVKiLavMy2-sd4nRS-jr7oq6-tASqG8BYvfQem9nI0w</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1563999963</pqid></control><display><type>article</type><title>class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant</title><source>MEDLINE</source><source>Jstor Complete Legacy</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Wei, Yifeng ; Funk, Michael A ; Rosado, Leonardo A ; Baek, Jiyeon ; Drennan, Catherine L ; Stubbe, JoAnne</creator><creatorcontrib>Wei, Yifeng ; Funk, Michael A ; Rosado, Leonardo A ; Baek, Jiyeon ; Drennan, Catherine L ; Stubbe, JoAnne</creatorcontrib><description>Significance Ribonucleotide reductases (RNRs) catalyze nucleotide reduction via complex radical chemistry, providing deoxynucleotides for DNA synthesis in all domains of life. Many anaerobic bacteria and archaea contain the class III O ₂-sensitive RNR, and those that have been studied to date couple nucleotide reduction to formate oxidation. Here we report the characterization of a second class III RNR subtype that couples nucleotide reduction to the oxidation of thioredoxin. Because of the central role of formate and thiols in many anaerobic processes, the distribution of class III RNRs among different organisms may shed light on aspects of anaerobic biochemistry.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.1414396111</identifier><identifier>PMID: 25157154</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Amino Acids - metabolism ; Archaea ; Bacteria ; Biocatalysis ; Biological Sciences ; Catalytic Domain ; Cloning ; Computational Biology ; Crystallography, X-Ray ; Cytidine Triphosphate - metabolism ; Cytosine - metabolism ; Disulfides - metabolism ; DNA ; Electron Spin Resonance Spectroscopy ; Enzymes ; formates ; Metabolism ; Models, Biological ; NADP ; Neisseria ; Neisseria - enzymology ; Oxidation ; Oxidation-Reduction ; Phylogenetics ; PNAS Plus ; reducing agents ; Reducing Agents - metabolism ; ribonucleotide reductase ; Ribonucleotide Reductases - chemistry ; Ribonucleotide Reductases - metabolism ; Thermotoga maritima ; Thermotoga maritima - enzymology ; thiols ; Thioredoxins - metabolism ; Time Factors</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2014-09, Vol.111 (36), p.E3756-E3765</ispartof><rights>Copyright National Academy of Sciences Sep 9, 2014</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c536t-c1093b105cc899254b29ae2c336babc4e531391126bf171dfff3750cdcf159d83</citedby><cites>FETCH-LOGICAL-c536t-c1093b105cc899254b29ae2c336babc4e531391126bf171dfff3750cdcf159d83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/111/36.cover.gif</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4246965/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4246965/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,724,777,781,882,27905,27906,53772,53774</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25157154$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wei, Yifeng</creatorcontrib><creatorcontrib>Funk, Michael A</creatorcontrib><creatorcontrib>Rosado, Leonardo A</creatorcontrib><creatorcontrib>Baek, Jiyeon</creatorcontrib><creatorcontrib>Drennan, Catherine L</creatorcontrib><creatorcontrib>Stubbe, JoAnne</creatorcontrib><title>class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Significance Ribonucleotide reductases (RNRs) catalyze nucleotide reduction via complex radical chemistry, providing deoxynucleotides for DNA synthesis in all domains of life. Many anaerobic bacteria and archaea contain the class III O ₂-sensitive RNR, and those that have been studied to date couple nucleotide reduction to formate oxidation. Here we report the characterization of a second class III RNR subtype that couples nucleotide reduction to the oxidation of thioredoxin. Because of the central role of formate and thiols in many anaerobic processes, the distribution of class III RNRs among different organisms may shed light on aspects of anaerobic biochemistry.</description><subject>Amino Acids - metabolism</subject><subject>Archaea</subject><subject>Bacteria</subject><subject>Biocatalysis</subject><subject>Biological Sciences</subject><subject>Catalytic Domain</subject><subject>Cloning</subject><subject>Computational Biology</subject><subject>Crystallography, X-Ray</subject><subject>Cytidine Triphosphate - metabolism</subject><subject>Cytosine - metabolism</subject><subject>Disulfides - metabolism</subject><subject>DNA</subject><subject>Electron Spin Resonance Spectroscopy</subject><subject>Enzymes</subject><subject>formates</subject><subject>Metabolism</subject><subject>Models, Biological</subject><subject>NADP</subject><subject>Neisseria</subject><subject>Neisseria - enzymology</subject><subject>Oxidation</subject><subject>Oxidation-Reduction</subject><subject>Phylogenetics</subject><subject>PNAS Plus</subject><subject>reducing agents</subject><subject>Reducing Agents - metabolism</subject><subject>ribonucleotide reductase</subject><subject>Ribonucleotide Reductases - chemistry</subject><subject>Ribonucleotide Reductases - metabolism</subject><subject>Thermotoga maritima</subject><subject>Thermotoga maritima - enzymology</subject><subject>thiols</subject><subject>Thioredoxins - metabolism</subject><subject>Time Factors</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkr1vFDEQxS0EIkegpgNLNDSbeNYfu26QoijASREUkNryeu3Ekc8-7F0E-evj1V2OjwYsWS78mzczTw-hl0BOgHT0dBt1OQEGjEoBAI_QCoiERjBJHqMVIW3X9KxlR-hZKbeEEMl78hQdtRx4B5ytkDNBl4LX6zXOfkhxNsGmyY8WZzvOZtLFYpfTBn-yvhSbvcaDNj4E71Le-IKNjniefPB3Fk83PtWy9MNHrAvWDxpxeo6eOB2KfbF_j9HV-4uv5x-by88f1udnl43hVEyNqdPTAQg3ppey5WxopbatoVQMejDMcgpUArRicNDB6JyjHSdmNA64HHt6jN7tdLfzsLGjsXHKOqht9hudf6qkvfrzJ_obdZ2-q2qSkIJXgbd7gZy-zbZMqi5pbAg62jQXBT2hpGeCkH-jXIieLlb_Dwq1fy9ERd_8hd6mOcdq2kJRWY-glTrdUSanUrJ1hxWBqCUZakmG-pWMWvHqd2cO_EMUKoD3wFJ5kANQVKiLavMy2-sd4nRS-jr7oq6-tASqG8BYvfQem9nI0w</recordid><startdate>20140909</startdate><enddate>20140909</enddate><creator>Wei, Yifeng</creator><creator>Funk, Michael A</creator><creator>Rosado, Leonardo A</creator><creator>Baek, Jiyeon</creator><creator>Drennan, Catherine L</creator><creator>Stubbe, JoAnne</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><scope>FBQ</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>7S9</scope><scope>L.6</scope><scope>5PM</scope></search><sort><creationdate>20140909</creationdate><title>class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant</title><author>Wei, Yifeng ; Funk, Michael A ; Rosado, Leonardo A ; Baek, Jiyeon ; Drennan, Catherine L ; Stubbe, JoAnne</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c536t-c1093b105cc899254b29ae2c336babc4e531391126bf171dfff3750cdcf159d83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Amino Acids - metabolism</topic><topic>Archaea</topic><topic>Bacteria</topic><topic>Biocatalysis</topic><topic>Biological Sciences</topic><topic>Catalytic Domain</topic><topic>Cloning</topic><topic>Computational Biology</topic><topic>Crystallography, X-Ray</topic><topic>Cytidine Triphosphate - metabolism</topic><topic>Cytosine - metabolism</topic><topic>Disulfides - metabolism</topic><topic>DNA</topic><topic>Electron Spin Resonance Spectroscopy</topic><topic>Enzymes</topic><topic>formates</topic><topic>Metabolism</topic><topic>Models, Biological</topic><topic>NADP</topic><topic>Neisseria</topic><topic>Neisseria - enzymology</topic><topic>Oxidation</topic><topic>Oxidation-Reduction</topic><topic>Phylogenetics</topic><topic>PNAS Plus</topic><topic>reducing agents</topic><topic>Reducing Agents - metabolism</topic><topic>ribonucleotide reductase</topic><topic>Ribonucleotide Reductases - chemistry</topic><topic>Ribonucleotide Reductases - metabolism</topic><topic>Thermotoga maritima</topic><topic>Thermotoga maritima - enzymology</topic><topic>thiols</topic><topic>Thioredoxins - metabolism</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wei, Yifeng</creatorcontrib><creatorcontrib>Funk, Michael A</creatorcontrib><creatorcontrib>Rosado, Leonardo A</creatorcontrib><creatorcontrib>Baek, Jiyeon</creatorcontrib><creatorcontrib>Drennan, Catherine L</creatorcontrib><creatorcontrib>Stubbe, JoAnne</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium &amp; Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wei, Yifeng</au><au>Funk, Michael A</au><au>Rosado, Leonardo A</au><au>Baek, Jiyeon</au><au>Drennan, Catherine L</au><au>Stubbe, JoAnne</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2014-09-09</date><risdate>2014</risdate><volume>111</volume><issue>36</issue><spage>E3756</spage><epage>E3765</epage><pages>E3756-E3765</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Significance Ribonucleotide reductases (RNRs) catalyze nucleotide reduction via complex radical chemistry, providing deoxynucleotides for DNA synthesis in all domains of life. Many anaerobic bacteria and archaea contain the class III O ₂-sensitive RNR, and those that have been studied to date couple nucleotide reduction to formate oxidation. Here we report the characterization of a second class III RNR subtype that couples nucleotide reduction to the oxidation of thioredoxin. Because of the central role of formate and thiols in many anaerobic processes, the distribution of class III RNRs among different organisms may shed light on aspects of anaerobic biochemistry.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>25157154</pmid><doi>10.1073/pnas.1414396111</doi><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0027-8424
ispartof Proceedings of the National Academy of Sciences - PNAS, 2014-09, Vol.111 (36), p.E3756-E3765
issn 0027-8424
1091-6490
language eng
recordid cdi_pnas_primary_111_36_E3756
source MEDLINE; Jstor Complete Legacy; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry
subjects Amino Acids - metabolism
Archaea
Bacteria
Biocatalysis
Biological Sciences
Catalytic Domain
Cloning
Computational Biology
Crystallography, X-Ray
Cytidine Triphosphate - metabolism
Cytosine - metabolism
Disulfides - metabolism
DNA
Electron Spin Resonance Spectroscopy
Enzymes
formates
Metabolism
Models, Biological
NADP
Neisseria
Neisseria - enzymology
Oxidation
Oxidation-Reduction
Phylogenetics
PNAS Plus
reducing agents
Reducing Agents - metabolism
ribonucleotide reductase
Ribonucleotide Reductases - chemistry
Ribonucleotide Reductases - metabolism
Thermotoga maritima
Thermotoga maritima - enzymology
thiols
Thioredoxins - metabolism
Time Factors
title class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-18T10%3A29%3A45IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pnas_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=class%20III%20ribonucleotide%20reductase%20from%20Neisseria%20bacilliformis%20can%20utilize%20thioredoxin%20as%20a%20reductant&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20-%20PNAS&rft.au=Wei,%20Yifeng&rft.date=2014-09-09&rft.volume=111&rft.issue=36&rft.spage=E3756&rft.epage=E3765&rft.pages=E3756-E3765&rft.issn=0027-8424&rft.eissn=1091-6490&rft_id=info:doi/10.1073/pnas.1414396111&rft_dat=%3Cproquest_pnas_%3E1803084600%3C/proquest_pnas_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1563999963&rft_id=info:pmid/25157154&rfr_iscdi=true