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...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2014-09, Vol.111 (36), p.E3756-E3765 |
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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. |
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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. 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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 |
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