Loading…

Artificial Metalloenzymes for Enantioselective Catalysis Based on Biotin−Avidin

Homogeneous and enzymatic catalysis offer complementary means to generate enantiomerically pure compounds. Incorporation of achiral biotinylated rhodium−diphosphine complexes into (strept)avidin yields artificial metalloenzymes for the hydrogenation of N-protected dehydroamino acids. A chemogenetic...

Full description

Saved in:

Bibliographic Details
Published in:	Journal of the American Chemical Society 2003-07, Vol.125 (30), p.9030-9031
Main Authors:	Collot, Jérôme, Gradinaru, Julieta, Humbert, Nicolas, Skander, Myriem, Zocchi, Andrea, Ward, Thomas R
Format:	Article
Language:	English
Subjects:	Acrylates - chemistry Analytical, structural and metabolic biochemistry Avidin - chemistry Biological and medical sciences Biotin - chemistry Catalysis Cinnamates - chemistry Enzymes - chemistry Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrogenation Metalloproteins - chemistry Miscellaneous Rhodium - chemistry Stereoisomerism Streptavidin - chemistry Substrate Specificity
Citations:	Items that this one cites Items that cite this one
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

cited_by	cdi_FETCH-LOGICAL-a379t-69af67a5ed5049a55e5b7a512e43e141b184fb069475cfedd5e5c4cd3f714e023
cites	cdi_FETCH-LOGICAL-a379t-69af67a5ed5049a55e5b7a512e43e141b184fb069475cfedd5e5c4cd3f714e023
container_end_page	9031
container_issue	30
container_start_page	9030
container_title	Journal of the American Chemical Society
container_volume	125
creator	Collot, Jérôme Gradinaru, Julieta Humbert, Nicolas Skander, Myriem Zocchi, Andrea Ward, Thomas R
description	Homogeneous and enzymatic catalysis offer complementary means to generate enantiomerically pure compounds. Incorporation of achiral biotinylated rhodium−diphosphine complexes into (strept)avidin yields artificial metalloenzymes for the hydrogenation of N-protected dehydroamino acids. A chemogenetic optimization procedure allows one to produce (R)-acetamidoalanine with 96% enantioselectivity. These hybrid catalysts display features reminiscent both of enzymatic and of homogeneous systems.
doi_str_mv	10.1021/ja035545i
format	article
fullrecord	<record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_71588366</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>71588366</sourcerecordid><originalsourceid>FETCH-LOGICAL-a379t-69af67a5ed5049a55e5b7a512e43e141b184fb069475cfedd5e5c4cd3f714e023</originalsourceid><addsrcrecordid>eNpt0M9OFEEQBvCOkcgKHnwBMxdNOIz0_5k5LguoCQgqxmOntqc66XW2G7tnicsTeOYRfRKb7AY8cKpU6pcvlY-Q14y-Z5SzwwVQoZRU_hmZMMVprRjXz8mEUsrrptVil7zMeVFWyVv2guwyJXQnlJ6QL9M0eueth6E6xxGGIWK4XS8xVy6m6iRAGH3MOKAd_Q1WMyhmnX2ujiBjX8VQHfk4-vD3z930xvc-7JMdB0PGV9u5R76fnlzNPtZnFx8-zaZnNYimG2vdgdMNKOwVlR0ohWpeVsZRCmSSzVkr3ZzqTjbKOuz7Aqy0vXANk0i52CPvNrnXKf5aYR7N0meLwwAB4yqbhqm2FVoXeLCBNsWcEzpznfwS0towau77Mw_9FftmG7qaL7F_lNvCCni7BZAtDC5BsD7_5yinQnbF1Rvn84i_H-6QfhrdiEaZq8tv5vSr_HE8-8xN-5gLNptFXKVQunviwX-KNJQW</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>71588366</pqid></control><display><type>article</type><title>Artificial Metalloenzymes for Enantioselective Catalysis Based on Biotin−Avidin</title><source>American Chemical Society:Jisc Collections:American Chemical Society Read & Publish Agreement 2022-2024 (Reading list)</source><creator>Collot, Jérôme ; Gradinaru, Julieta ; Humbert, Nicolas ; Skander, Myriem ; Zocchi, Andrea ; Ward, Thomas R</creator><creatorcontrib>Collot, Jérôme ; Gradinaru, Julieta ; Humbert, Nicolas ; Skander, Myriem ; Zocchi, Andrea ; Ward, Thomas R</creatorcontrib><description>Homogeneous and enzymatic catalysis offer complementary means to generate enantiomerically pure compounds. Incorporation of achiral biotinylated rhodium−diphosphine complexes into (strept)avidin yields artificial metalloenzymes for the hydrogenation of N-protected dehydroamino acids. A chemogenetic optimization procedure allows one to produce (R)-acetamidoalanine with 96% enantioselectivity. These hybrid catalysts display features reminiscent both of enzymatic and of homogeneous systems.</description><identifier>ISSN: 0002-7863</identifier><identifier>EISSN: 1520-5126</identifier><identifier>DOI: 10.1021/ja035545i</identifier><identifier>PMID: 15369356</identifier><identifier>CODEN: JACSAT</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Acrylates - chemistry ; Analytical, structural and metabolic biochemistry ; Avidin - chemistry ; Biological and medical sciences ; Biotin - chemistry ; Catalysis ; Cinnamates - chemistry ; Enzymes - chemistry ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Hydrogenation ; Metalloproteins - chemistry ; Miscellaneous ; Rhodium - chemistry ; Stereoisomerism ; Streptavidin - chemistry ; Substrate Specificity</subject><ispartof>Journal of the American Chemical Society, 2003-07, Vol.125 (30), p.9030-9031</ispartof><rights>Copyright © 2003 American Chemical Society</rights><rights>2004 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a379t-69af67a5ed5049a55e5b7a512e43e141b184fb069475cfedd5e5c4cd3f714e023</citedby><cites>FETCH-LOGICAL-a379t-69af67a5ed5049a55e5b7a512e43e141b184fb069475cfedd5e5c4cd3f714e023</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15020349$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15369356$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Collot, Jérôme</creatorcontrib><creatorcontrib>Gradinaru, Julieta</creatorcontrib><creatorcontrib>Humbert, Nicolas</creatorcontrib><creatorcontrib>Skander, Myriem</creatorcontrib><creatorcontrib>Zocchi, Andrea</creatorcontrib><creatorcontrib>Ward, Thomas R</creatorcontrib><title>Artificial Metalloenzymes for Enantioselective Catalysis Based on Biotin−Avidin</title><title>Journal of the American Chemical Society</title><addtitle>J. Am. Chem. Soc</addtitle><description>Homogeneous and enzymatic catalysis offer complementary means to generate enantiomerically pure compounds. Incorporation of achiral biotinylated rhodium−diphosphine complexes into (strept)avidin yields artificial metalloenzymes for the hydrogenation of N-protected dehydroamino acids. A chemogenetic optimization procedure allows one to produce (R)-acetamidoalanine with 96% enantioselectivity. These hybrid catalysts display features reminiscent both of enzymatic and of homogeneous systems.</description><subject>Acrylates - chemistry</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Avidin - chemistry</subject><subject>Biological and medical sciences</subject><subject>Biotin - chemistry</subject><subject>Catalysis</subject><subject>Cinnamates - chemistry</subject><subject>Enzymes - chemistry</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogenation</subject><subject>Metalloproteins - chemistry</subject><subject>Miscellaneous</subject><subject>Rhodium - chemistry</subject><subject>Stereoisomerism</subject><subject>Streptavidin - chemistry</subject><subject>Substrate Specificity</subject><issn>0002-7863</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><recordid>eNpt0M9OFEEQBvCOkcgKHnwBMxdNOIz0_5k5LguoCQgqxmOntqc66XW2G7tnicsTeOYRfRKb7AY8cKpU6pcvlY-Q14y-Z5SzwwVQoZRU_hmZMMVprRjXz8mEUsrrptVil7zMeVFWyVv2guwyJXQnlJ6QL9M0eueth6E6xxGGIWK4XS8xVy6m6iRAGH3MOKAd_Q1WMyhmnX2ujiBjX8VQHfk4-vD3z930xvc-7JMdB0PGV9u5R76fnlzNPtZnFx8-zaZnNYimG2vdgdMNKOwVlR0ohWpeVsZRCmSSzVkr3ZzqTjbKOuz7Aqy0vXANk0i52CPvNrnXKf5aYR7N0meLwwAB4yqbhqm2FVoXeLCBNsWcEzpznfwS0towau77Mw_9FftmG7qaL7F_lNvCCni7BZAtDC5BsD7_5yinQnbF1Rvn84i_H-6QfhrdiEaZq8tv5vSr_HE8-8xN-5gLNptFXKVQunviwX-KNJQW</recordid><startdate>20030730</startdate><enddate>20030730</enddate><creator>Collot, Jérôme</creator><creator>Gradinaru, Julieta</creator><creator>Humbert, Nicolas</creator><creator>Skander, Myriem</creator><creator>Zocchi, Andrea</creator><creator>Ward, Thomas R</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>IQODW</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>7X8</scope></search><sort><creationdate>20030730</creationdate><title>Artificial Metalloenzymes for Enantioselective Catalysis Based on Biotin−Avidin</title><author>Collot, Jérôme ; Gradinaru, Julieta ; Humbert, Nicolas ; Skander, Myriem ; Zocchi, Andrea ; Ward, Thomas R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a379t-69af67a5ed5049a55e5b7a512e43e141b184fb069475cfedd5e5c4cd3f714e023</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Acrylates - chemistry</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Avidin - chemistry</topic><topic>Biological and medical sciences</topic><topic>Biotin - chemistry</topic><topic>Catalysis</topic><topic>Cinnamates - chemistry</topic><topic>Enzymes - chemistry</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrogenation</topic><topic>Metalloproteins - chemistry</topic><topic>Miscellaneous</topic><topic>Rhodium - chemistry</topic><topic>Stereoisomerism</topic><topic>Streptavidin - chemistry</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Collot, Jérôme</creatorcontrib><creatorcontrib>Gradinaru, Julieta</creatorcontrib><creatorcontrib>Humbert, Nicolas</creatorcontrib><creatorcontrib>Skander, Myriem</creatorcontrib><creatorcontrib>Zocchi, Andrea</creatorcontrib><creatorcontrib>Ward, Thomas R</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Collot, Jérôme</au><au>Gradinaru, Julieta</au><au>Humbert, Nicolas</au><au>Skander, Myriem</au><au>Zocchi, Andrea</au><au>Ward, Thomas R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Artificial Metalloenzymes for Enantioselective Catalysis Based on Biotin−Avidin</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>2003-07-30</date><risdate>2003</risdate><volume>125</volume><issue>30</issue><spage>9030</spage><epage>9031</epage><pages>9030-9031</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><coden>JACSAT</coden><abstract>Homogeneous and enzymatic catalysis offer complementary means to generate enantiomerically pure compounds. Incorporation of achiral biotinylated rhodium−diphosphine complexes into (strept)avidin yields artificial metalloenzymes for the hydrogenation of N-protected dehydroamino acids. A chemogenetic optimization procedure allows one to produce (R)-acetamidoalanine with 96% enantioselectivity. These hybrid catalysts display features reminiscent both of enzymatic and of homogeneous systems.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>15369356</pmid><doi>10.1021/ja035545i</doi><tpages>2</tpages></addata></record>
fulltext	fulltext
identifier	ISSN: 0002-7863
ispartof	Journal of the American Chemical Society, 2003-07, Vol.125 (30), p.9030-9031
issn	0002-7863 1520-5126
language	eng
recordid	cdi_proquest_miscellaneous_71588366
source	American Chemical Society:Jisc Collections:American Chemical Society Read & Publish Agreement 2022-2024 (Reading list)
subjects	Acrylates - chemistry Analytical, structural and metabolic biochemistry Avidin - chemistry Biological and medical sciences Biotin - chemistry Catalysis Cinnamates - chemistry Enzymes - chemistry Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrogenation Metalloproteins - chemistry Miscellaneous Rhodium - chemistry Stereoisomerism Streptavidin - chemistry Substrate Specificity
title	Artificial Metalloenzymes for Enantioselective Catalysis Based on Biotin−Avidin
url	http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-02T14%3A35%3A45IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Artificial%20Metalloenzymes%20for%20Enantioselective%20Catalysis%20Based%20on%20Biotin%E2%88%92Avidin&rft.jtitle=Journal%20of%20the%20American%20Chemical%20Society&rft.au=Collot,%20J%C3%A9r%C3%B4me&rft.date=2003-07-30&rft.volume=125&rft.issue=30&rft.spage=9030&rft.epage=9031&rft.pages=9030-9031&rft.issn=0002-7863&rft.eissn=1520-5126&rft.coden=JACSAT&rft_id=info:doi/10.1021/ja035545i&rft_dat=%3Cproquest_cross%3E71588366%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-a379t-69af67a5ed5049a55e5b7a512e43e141b184fb069475cfedd5e5c4cd3f714e023%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=71588366&rft_id=info:pmid/15369356&rfr_iscdi=true