Hg-C bond protonolysis by a functional model of bacterial enzyme organomercurial lyase MerB
Herein, we report a novel synthetic compound 1 , having a highly nucleophilic selenolate (Se − ) moiety and a thiol (-SH) functional group, which showed efficient Hg-C bond protonolysis of various R-Hg-X molecules including neurotoxic methylmercury and thimerosal, via direct -SH proton transfer to t...
Gespeichert in:
| Veröffentlicht in: | Chemical communications (Cambridge, England) England), 2020-08, Vol.56 (65), p.928-9283 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 9283 |
|---|---|
| container_issue | 65 |
| container_start_page | 928 |
| container_title | Chemical communications (Cambridge, England) |
| container_volume | 56 |
| creator | Karri, Ramesh Das, Ranajit Rai, Rakesh Kumar Gopalakrishnan, Anaswara Roy, Gouriprasanna |
| description | Herein, we report a novel synthetic compound
1
, having a highly nucleophilic selenolate (Se
−
) moiety and a thiol (-SH) functional group, which showed efficient Hg-C bond protonolysis of various R-Hg-X molecules including neurotoxic methylmercury and thimerosal,
via
direct -SH proton transfer to the highly activated C-atom of a departed R group with low activation energy barrier at room temperature (21 °C), in the absence of any external proton source and, thus, acts as a functional model of MerB.
We report a synthetic molecule
1
, which shows a remarkable ability to protolytically cleave the Hg-C bonds of a wide variety of organomercurials to hydrocarbon and Hg
2+
products under mild conditions, similar to the bacterial enzyme MerB. |
| doi_str_mv | 10.1039/d0cc02232b |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmed_primary_32558833</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2433201106</sourcerecordid><originalsourceid>FETCH-LOGICAL-c474t-4bca34efe8ec8943f1145ebb44c427c2b786fcee3505ea5b7754d7ab3628f79b3</originalsourceid><addsrcrecordid>eNp9kctLw0AQxhdRbK1evCsr3oToPpv0aOMTKl4UBA9hdzNbUpJs3U0O8a83fVhvzmWGb34MM98gdErJNSV8cpMTYwhjnOk9NKR8LCIpko_9VS0nUcyFHKCjEBakDyqTQzTgTMok4XyIPp_mUYq1q3O89K5xtSu7UASsO6ywbWvTFK5WJa5cDiV2FmtlGvBFL0H93VWAnZ-r2lXgTbuWy04FwC_gp8fowKoywMk2j9D7w_1b-hTNXh-f09tZZEQsmkhoo7gACwmYZCK4pVRI0FoII1hsmI6TsTUAXBIJSuo4liKPleZjlth4ovkIXW7m9hd8tRCabOFa328dMiY4Z4RSMu6pqw1lvAvBg82WvqiU7zJKspWP2R1J07WP0x4-345sdQX5Dv01rgcuNoAPZtf9e0S2zG3PnP3H8B91goMA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2433201106</pqid></control><display><type>article</type><title>Hg-C bond protonolysis by a functional model of bacterial enzyme organomercurial lyase MerB</title><source>MEDLINE</source><source>Royal Society Of Chemistry Journals 2008-</source><source>Alma/SFX Local Collection</source><creator>Karri, Ramesh ; Das, Ranajit ; Rai, Rakesh Kumar ; Gopalakrishnan, Anaswara ; Roy, Gouriprasanna</creator><creatorcontrib>Karri, Ramesh ; Das, Ranajit ; Rai, Rakesh Kumar ; Gopalakrishnan, Anaswara ; Roy, Gouriprasanna</creatorcontrib><description>Herein, we report a novel synthetic compound
1
, having a highly nucleophilic selenolate (Se
−
) moiety and a thiol (-SH) functional group, which showed efficient Hg-C bond protonolysis of various R-Hg-X molecules including neurotoxic methylmercury and thimerosal,
via
direct -SH proton transfer to the highly activated C-atom of a departed R group with low activation energy barrier at room temperature (21 °C), in the absence of any external proton source and, thus, acts as a functional model of MerB.
We report a synthetic molecule
1
, which shows a remarkable ability to protolytically cleave the Hg-C bonds of a wide variety of organomercurials to hydrocarbon and Hg
2+
products under mild conditions, similar to the bacterial enzyme MerB.</description><identifier>ISSN: 1359-7345</identifier><identifier>EISSN: 1364-548X</identifier><identifier>DOI: 10.1039/d0cc02232b</identifier><identifier>PMID: 32558833</identifier><language>eng</language><publisher>England: Royal Society of Chemistry</publisher><subject>Bacterial Proteins - chemistry ; Bacterial Proteins - metabolism ; Carbon - chemistry ; Crystallography ; Functional groups ; Lyases - chemistry ; Lyases - metabolism ; Mercury (metal) ; Mercury - chemistry ; Models, Molecular ; NMR ; Nuclear magnetic resonance ; Protons ; Room temperature ; Selenium ; Selenium Compounds - chemistry ; Sulfhydryl Compounds - chemistry ; Temperature</subject><ispartof>Chemical communications (Cambridge, England), 2020-08, Vol.56 (65), p.928-9283</ispartof><rights>Copyright Royal Society of Chemistry 2020</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c474t-4bca34efe8ec8943f1145ebb44c427c2b786fcee3505ea5b7754d7ab3628f79b3</citedby><cites>FETCH-LOGICAL-c474t-4bca34efe8ec8943f1145ebb44c427c2b786fcee3505ea5b7754d7ab3628f79b3</cites><orcidid>0000-0002-0047-3575</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32558833$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Karri, Ramesh</creatorcontrib><creatorcontrib>Das, Ranajit</creatorcontrib><creatorcontrib>Rai, Rakesh Kumar</creatorcontrib><creatorcontrib>Gopalakrishnan, Anaswara</creatorcontrib><creatorcontrib>Roy, Gouriprasanna</creatorcontrib><title>Hg-C bond protonolysis by a functional model of bacterial enzyme organomercurial lyase MerB</title><title>Chemical communications (Cambridge, England)</title><addtitle>Chem Commun (Camb)</addtitle><description>Herein, we report a novel synthetic compound
1
, having a highly nucleophilic selenolate (Se
−
) moiety and a thiol (-SH) functional group, which showed efficient Hg-C bond protonolysis of various R-Hg-X molecules including neurotoxic methylmercury and thimerosal,
via
direct -SH proton transfer to the highly activated C-atom of a departed R group with low activation energy barrier at room temperature (21 °C), in the absence of any external proton source and, thus, acts as a functional model of MerB.
We report a synthetic molecule
1
, which shows a remarkable ability to protolytically cleave the Hg-C bonds of a wide variety of organomercurials to hydrocarbon and Hg
2+
products under mild conditions, similar to the bacterial enzyme MerB.</description><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>Carbon - chemistry</subject><subject>Crystallography</subject><subject>Functional groups</subject><subject>Lyases - chemistry</subject><subject>Lyases - metabolism</subject><subject>Mercury (metal)</subject><subject>Mercury - chemistry</subject><subject>Models, Molecular</subject><subject>NMR</subject><subject>Nuclear magnetic resonance</subject><subject>Protons</subject><subject>Room temperature</subject><subject>Selenium</subject><subject>Selenium Compounds - chemistry</subject><subject>Sulfhydryl Compounds - chemistry</subject><subject>Temperature</subject><issn>1359-7345</issn><issn>1364-548X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kctLw0AQxhdRbK1evCsr3oToPpv0aOMTKl4UBA9hdzNbUpJs3U0O8a83fVhvzmWGb34MM98gdErJNSV8cpMTYwhjnOk9NKR8LCIpko_9VS0nUcyFHKCjEBakDyqTQzTgTMok4XyIPp_mUYq1q3O89K5xtSu7UASsO6ywbWvTFK5WJa5cDiV2FmtlGvBFL0H93VWAnZ-r2lXgTbuWy04FwC_gp8fowKoywMk2j9D7w_1b-hTNXh-f09tZZEQsmkhoo7gACwmYZCK4pVRI0FoII1hsmI6TsTUAXBIJSuo4liKPleZjlth4ovkIXW7m9hd8tRCabOFa328dMiY4Z4RSMu6pqw1lvAvBg82WvqiU7zJKspWP2R1J07WP0x4-345sdQX5Dv01rgcuNoAPZtf9e0S2zG3PnP3H8B91goMA</recordid><startdate>20200821</startdate><enddate>20200821</enddate><creator>Karri, Ramesh</creator><creator>Das, Ranajit</creator><creator>Rai, Rakesh Kumar</creator><creator>Gopalakrishnan, Anaswara</creator><creator>Roy, Gouriprasanna</creator><general>Royal Society of Chemistry</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>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope><orcidid>https://orcid.org/0000-0002-0047-3575</orcidid></search><sort><creationdate>20200821</creationdate><title>Hg-C bond protonolysis by a functional model of bacterial enzyme organomercurial lyase MerB</title><author>Karri, Ramesh ; Das, Ranajit ; Rai, Rakesh Kumar ; Gopalakrishnan, Anaswara ; Roy, Gouriprasanna</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c474t-4bca34efe8ec8943f1145ebb44c427c2b786fcee3505ea5b7754d7ab3628f79b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - metabolism</topic><topic>Carbon - chemistry</topic><topic>Crystallography</topic><topic>Functional groups</topic><topic>Lyases - chemistry</topic><topic>Lyases - metabolism</topic><topic>Mercury (metal)</topic><topic>Mercury - chemistry</topic><topic>Models, Molecular</topic><topic>NMR</topic><topic>Nuclear magnetic resonance</topic><topic>Protons</topic><topic>Room temperature</topic><topic>Selenium</topic><topic>Selenium Compounds - chemistry</topic><topic>Sulfhydryl Compounds - chemistry</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Karri, Ramesh</creatorcontrib><creatorcontrib>Das, Ranajit</creatorcontrib><creatorcontrib>Rai, Rakesh Kumar</creatorcontrib><creatorcontrib>Gopalakrishnan, Anaswara</creatorcontrib><creatorcontrib>Roy, Gouriprasanna</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Engineered Materials Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Chemical communications (Cambridge, England)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Karri, Ramesh</au><au>Das, Ranajit</au><au>Rai, Rakesh Kumar</au><au>Gopalakrishnan, Anaswara</au><au>Roy, Gouriprasanna</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Hg-C bond protonolysis by a functional model of bacterial enzyme organomercurial lyase MerB</atitle><jtitle>Chemical communications (Cambridge, England)</jtitle><addtitle>Chem Commun (Camb)</addtitle><date>2020-08-21</date><risdate>2020</risdate><volume>56</volume><issue>65</issue><spage>928</spage><epage>9283</epage><pages>928-9283</pages><issn>1359-7345</issn><eissn>1364-548X</eissn><abstract>Herein, we report a novel synthetic compound
1
, having a highly nucleophilic selenolate (Se
−
) moiety and a thiol (-SH) functional group, which showed efficient Hg-C bond protonolysis of various R-Hg-X molecules including neurotoxic methylmercury and thimerosal,
via
direct -SH proton transfer to the highly activated C-atom of a departed R group with low activation energy barrier at room temperature (21 °C), in the absence of any external proton source and, thus, acts as a functional model of MerB.
We report a synthetic molecule
1
, which shows a remarkable ability to protolytically cleave the Hg-C bonds of a wide variety of organomercurials to hydrocarbon and Hg
2+
products under mild conditions, similar to the bacterial enzyme MerB.</abstract><cop>England</cop><pub>Royal Society of Chemistry</pub><pmid>32558833</pmid><doi>10.1039/d0cc02232b</doi><tpages>4</tpages><orcidid>https://orcid.org/0000-0002-0047-3575</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1359-7345 |
| ispartof | Chemical communications (Cambridge, England), 2020-08, Vol.56 (65), p.928-9283 |
| issn | 1359-7345 1364-548X |
| language | eng |
| recordid | cdi_pubmed_primary_32558833 |
| source | MEDLINE; Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
| subjects | Bacterial Proteins - chemistry Bacterial Proteins - metabolism Carbon - chemistry Crystallography Functional groups Lyases - chemistry Lyases - metabolism Mercury (metal) Mercury - chemistry Models, Molecular NMR Nuclear magnetic resonance Protons Room temperature Selenium Selenium Compounds - chemistry Sulfhydryl Compounds - chemistry Temperature |
| title | Hg-C bond protonolysis by a functional model of bacterial enzyme organomercurial lyase MerB |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-27T05%3A30%3A49IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Hg-C%20bond%20protonolysis%20by%20a%20functional%20model%20of%20bacterial%20enzyme%20organomercurial%20lyase%20MerB&rft.jtitle=Chemical%20communications%20(Cambridge,%20England)&rft.au=Karri,%20Ramesh&rft.date=2020-08-21&rft.volume=56&rft.issue=65&rft.spage=928&rft.epage=9283&rft.pages=928-9283&rft.issn=1359-7345&rft.eissn=1364-548X&rft_id=info:doi/10.1039/d0cc02232b&rft_dat=%3Cproquest_pubme%3E2433201106%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2433201106&rft_id=info:pmid/32558833&rfr_iscdi=true |