Reactivity studies of the tyrosyl radical in ribonucleotide reductase from Mycobacterium tuberculosis and Arabidopsis thaliana: comparison with Escherichia coli and mouse
Ribonucleotide reductase (RNR) is a key enzyme for DNA synthesis since it provides cells with deoxyribonucleotides, the DNA precursors. Class I alpha2beta2 RNRs contain a dinuclear iron center and an essential tyrosyl radical in the beta2 component (protein R2). This is also true for the purified pr...
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| Veröffentlicht in: | European Journal of Biochemistry 1998-12, Vol.258 (2), p.485-490 |
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| container_title | European Journal of Biochemistry |
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| creator | Elleingand, E Gerez, C Un, S Knupling, M Lu, G Salem, J Rubin, H Sauge-Merle, S Laulhere, J.P Fontecave, M |
| description | Ribonucleotide reductase (RNR) is a key enzyme for DNA synthesis since it provides cells with deoxyribonucleotides, the DNA precursors. Class I alpha2beta2 RNRs contain a dinuclear iron center and an essential tyrosyl radical in the beta2 component (protein R2). This is also true for the purified protein R2 of Mycobacterium tuberculosis RNR, as shown by iron analysis, light absorption and EPR spectroscopy. EPR spectroscopy at 286 GHz revealed a high g(x) value, suggesting that the radical is not hydrogen bonded, as in other prokaryotic R2s and in contrast with eukaryotic R2s (from Arabidopsis thaliana and mouse). Furthermore, it proved to be very resistant to scavenging by a variety of phenols and thiols and by hydroxyurea, similar to the Escherichia coli radical. By comparison, the plant and mouse radicals are very sensitive to drugs such as resveratrol and 2-thiophenthiol. The radical from M. tuberculosis RNR does not seem to be an appropriate target for new antituberculous agents. |
| doi_str_mv | 10.1046/j.1432-1327.1998.2580485.x |
| format | Article |
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Class I alpha2beta2 RNRs contain a dinuclear iron center and an essential tyrosyl radical in the beta2 component (protein R2). This is also true for the purified protein R2 of Mycobacterium tuberculosis RNR, as shown by iron analysis, light absorption and EPR spectroscopy. EPR spectroscopy at 286 GHz revealed a high g(x) value, suggesting that the radical is not hydrogen bonded, as in other prokaryotic R2s and in contrast with eukaryotic R2s (from Arabidopsis thaliana and mouse). Furthermore, it proved to be very resistant to scavenging by a variety of phenols and thiols and by hydroxyurea, similar to the Escherichia coli radical. By comparison, the plant and mouse radicals are very sensitive to drugs such as resveratrol and 2-thiophenthiol. The radical from M. tuberculosis RNR does not seem to be an appropriate target for new antituberculous agents.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>EISSN: 1432-1327</identifier><identifier>DOI: 10.1046/j.1432-1327.1998.2580485.x</identifier><identifier>PMID: 9874215</identifier><language>eng</language><publisher>England: Wiley</publisher><subject>animal diseases ; animal health ; Animals ; AR2 protein ; Arabidopsis - enzymology ; Arabidopsis thaliana ; bacterial infections ; Bacterial Proteins - chemistry ; Electron Spin Resonance Spectroscopy ; Escherichia coli ; Escherichia coli - enzymology ; Free Radical Scavengers - metabolism ; Free Radicals - metabolism ; human health and safety ; Iron - chemistry ; Life Sciences ; medicine ; Mice ; Mycobacterium tuberculosis ; Mycobacterium tuberculosis - enzymology ; plant biochemistry ; plant physiology ; Plant Proteins - chemistry ; Ribonucleotide Reductases - chemistry ; Spectrophotometry ; Tyrosine - metabolism ; tyrosyl radical</subject><ispartof>European Journal of Biochemistry, 1998-12, Vol.258 (2), p.485-490</ispartof><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><orcidid>0000-0002-8016-4747 ; 0000-0003-2721-3885</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/9874215$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://amu.hal.science/hal-01561220$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Elleingand, E</creatorcontrib><creatorcontrib>Gerez, C</creatorcontrib><creatorcontrib>Un, S</creatorcontrib><creatorcontrib>Knupling, M</creatorcontrib><creatorcontrib>Lu, G</creatorcontrib><creatorcontrib>Salem, J</creatorcontrib><creatorcontrib>Rubin, H</creatorcontrib><creatorcontrib>Sauge-Merle, S</creatorcontrib><creatorcontrib>Laulhere, J.P</creatorcontrib><creatorcontrib>Fontecave, M</creatorcontrib><title>Reactivity studies of the tyrosyl radical in ribonucleotide reductase from Mycobacterium tuberculosis and Arabidopsis thaliana: comparison with Escherichia coli and mouse</title><title>European Journal of Biochemistry</title><addtitle>Eur J Biochem</addtitle><description>Ribonucleotide reductase (RNR) is a key enzyme for DNA synthesis since it provides cells with deoxyribonucleotides, the DNA precursors. Class I alpha2beta2 RNRs contain a dinuclear iron center and an essential tyrosyl radical in the beta2 component (protein R2). This is also true for the purified protein R2 of Mycobacterium tuberculosis RNR, as shown by iron analysis, light absorption and EPR spectroscopy. EPR spectroscopy at 286 GHz revealed a high g(x) value, suggesting that the radical is not hydrogen bonded, as in other prokaryotic R2s and in contrast with eukaryotic R2s (from Arabidopsis thaliana and mouse). Furthermore, it proved to be very resistant to scavenging by a variety of phenols and thiols and by hydroxyurea, similar to the Escherichia coli radical. By comparison, the plant and mouse radicals are very sensitive to drugs such as resveratrol and 2-thiophenthiol. The radical from M. tuberculosis RNR does not seem to be an appropriate target for new antituberculous agents.</description><subject>animal diseases</subject><subject>animal health</subject><subject>Animals</subject><subject>AR2 protein</subject><subject>Arabidopsis - enzymology</subject><subject>Arabidopsis thaliana</subject><subject>bacterial infections</subject><subject>Bacterial Proteins - chemistry</subject><subject>Electron Spin Resonance Spectroscopy</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>Free Radical Scavengers - metabolism</subject><subject>Free Radicals - metabolism</subject><subject>human health and safety</subject><subject>Iron - chemistry</subject><subject>Life Sciences</subject><subject>medicine</subject><subject>Mice</subject><subject>Mycobacterium tuberculosis</subject><subject>Mycobacterium tuberculosis - enzymology</subject><subject>plant biochemistry</subject><subject>plant physiology</subject><subject>Plant Proteins - chemistry</subject><subject>Ribonucleotide Reductases - chemistry</subject><subject>Spectrophotometry</subject><subject>Tyrosine - metabolism</subject><subject>tyrosyl radical</subject><issn>0014-2956</issn><issn>1432-1033</issn><issn>1432-1327</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1u1DAUhS0EKkPhERAWCyQWCf6Jk7i7UVUo0iAkoGvrxnGIR0k82E5pXomnxCGjbllZ9jn3-Oh-CL2lJKekKD8cc1pwllHOqpxKWedM1KSoRf7wBO02iXD-FO0IoUXGpCifoxchHAkhpSyrC3Qh66pgVOzQn28GdLT3Ni44xLm1JmDX4dgbHBfvwjJgD63VMGA7YW8bN816MC7a1mBv2llHCAZ33o34y6Jdk9KMt_OI49wYr-fBBRswTC3ee2hs607rPfYwWJjgCms3nsDb4Cb828Ye3wTdpwDdW0jaYP-Njm4O5iV61sEQzKvzeYnuPt78uL7NDl8_fb7eHzLNizJmgnMqSm4YZx00jak0acquAV4LwirZsU6AbGtNeceNSHJRtI3W0IqSsqJm_BK933JTR3XydgS_KAdW3e4Pan0jdLUyck-T993mPXn3azYhqtEGbYYBJpM6q1LSZJbkv0a68uBiTbzajDptP3jTPVagRK301VGtiNVKX6301Zm-ekjDr8-_zM1o2sfRM-6kv9n0DpyCn2nt6u47I5QTVkvOC8n_Agz5uVw</recordid><startdate>19981201</startdate><enddate>19981201</enddate><creator>Elleingand, E</creator><creator>Gerez, C</creator><creator>Un, S</creator><creator>Knupling, M</creator><creator>Lu, G</creator><creator>Salem, J</creator><creator>Rubin, H</creator><creator>Sauge-Merle, S</creator><creator>Laulhere, J.P</creator><creator>Fontecave, M</creator><general>Wiley</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>7QL</scope><scope>C1K</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0002-8016-4747</orcidid><orcidid>https://orcid.org/0000-0003-2721-3885</orcidid></search><sort><creationdate>19981201</creationdate><title>Reactivity studies of the tyrosyl radical in ribonucleotide reductase from Mycobacterium tuberculosis and Arabidopsis thaliana: comparison with Escherichia coli and mouse</title><author>Elleingand, E ; Gerez, C ; Un, S ; Knupling, M ; Lu, G ; Salem, J ; Rubin, H ; Sauge-Merle, S ; Laulhere, J.P ; Fontecave, M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c346t-5331563e232fabbe7c0b6fba3850279f2f5a9d8c13f3e5e7c44dbccad56124823</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>animal diseases</topic><topic>animal health</topic><topic>Animals</topic><topic>AR2 protein</topic><topic>Arabidopsis - enzymology</topic><topic>Arabidopsis thaliana</topic><topic>bacterial infections</topic><topic>Bacterial Proteins - chemistry</topic><topic>Electron Spin Resonance Spectroscopy</topic><topic>Escherichia coli</topic><topic>Escherichia coli - enzymology</topic><topic>Free Radical Scavengers - metabolism</topic><topic>Free Radicals - metabolism</topic><topic>human health and safety</topic><topic>Iron - chemistry</topic><topic>Life Sciences</topic><topic>medicine</topic><topic>Mice</topic><topic>Mycobacterium tuberculosis</topic><topic>Mycobacterium tuberculosis - enzymology</topic><topic>plant biochemistry</topic><topic>plant physiology</topic><topic>Plant Proteins - chemistry</topic><topic>Ribonucleotide Reductases - chemistry</topic><topic>Spectrophotometry</topic><topic>Tyrosine - metabolism</topic><topic>tyrosyl radical</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Elleingand, E</creatorcontrib><creatorcontrib>Gerez, C</creatorcontrib><creatorcontrib>Un, S</creatorcontrib><creatorcontrib>Knupling, M</creatorcontrib><creatorcontrib>Lu, G</creatorcontrib><creatorcontrib>Salem, J</creatorcontrib><creatorcontrib>Rubin, H</creatorcontrib><creatorcontrib>Sauge-Merle, S</creatorcontrib><creatorcontrib>Laulhere, J.P</creatorcontrib><creatorcontrib>Fontecave, M</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>European Journal of Biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Elleingand, E</au><au>Gerez, C</au><au>Un, S</au><au>Knupling, M</au><au>Lu, G</au><au>Salem, J</au><au>Rubin, H</au><au>Sauge-Merle, S</au><au>Laulhere, J.P</au><au>Fontecave, M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Reactivity studies of the tyrosyl radical in ribonucleotide reductase from Mycobacterium tuberculosis and Arabidopsis thaliana: comparison with Escherichia coli and mouse</atitle><jtitle>European Journal of Biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1998-12-01</date><risdate>1998</risdate><volume>258</volume><issue>2</issue><spage>485</spage><epage>490</epage><pages>485-490</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><eissn>1432-1327</eissn><abstract>Ribonucleotide reductase (RNR) is a key enzyme for DNA synthesis since it provides cells with deoxyribonucleotides, the DNA precursors. Class I alpha2beta2 RNRs contain a dinuclear iron center and an essential tyrosyl radical in the beta2 component (protein R2). This is also true for the purified protein R2 of Mycobacterium tuberculosis RNR, as shown by iron analysis, light absorption and EPR spectroscopy. EPR spectroscopy at 286 GHz revealed a high g(x) value, suggesting that the radical is not hydrogen bonded, as in other prokaryotic R2s and in contrast with eukaryotic R2s (from Arabidopsis thaliana and mouse). Furthermore, it proved to be very resistant to scavenging by a variety of phenols and thiols and by hydroxyurea, similar to the Escherichia coli radical. By comparison, the plant and mouse radicals are very sensitive to drugs such as resveratrol and 2-thiophenthiol. 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| ispartof | European Journal of Biochemistry, 1998-12, Vol.258 (2), p.485-490 |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection; SpringerLink Journals - AutoHoldings |
| subjects | animal diseases animal health Animals AR2 protein Arabidopsis - enzymology Arabidopsis thaliana bacterial infections Bacterial Proteins - chemistry Electron Spin Resonance Spectroscopy Escherichia coli Escherichia coli - enzymology Free Radical Scavengers - metabolism Free Radicals - metabolism human health and safety Iron - chemistry Life Sciences medicine Mice Mycobacterium tuberculosis Mycobacterium tuberculosis - enzymology plant biochemistry plant physiology Plant Proteins - chemistry Ribonucleotide Reductases - chemistry Spectrophotometry Tyrosine - metabolism tyrosyl radical |
| title | Reactivity studies of the tyrosyl radical in ribonucleotide reductase from Mycobacterium tuberculosis and Arabidopsis thaliana: comparison with Escherichia coli and mouse |
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