Hydrogen Bonding of 1,2-Azaborines in the Binding Cavity of T4 Lysozyme Mutants: Structures and Thermodynamics
Protein crystallography and calorimetry were used to characterize the binding of 1,2-azaborines to model cavities in T4 lysozyme in direct comparison to their carbonaceous counterparts. In the apolar L99A cavity, affinity for Ab dropped only slightly versus benzene. In the cavity designed to accommo...
Gespeichert in:
Veröffentlicht in: | Journal of the American Chemical Society 2016-09, Vol.138 (37), p.12021-12024 |
---|---|
Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 12024 |
---|---|
container_issue | 37 |
container_start_page | 12021 |
container_title | Journal of the American Chemical Society |
container_volume | 138 |
creator | Lee, Hyelee Fischer, Marcus Shoichet, Brian K Liu, Shih-Yuan |
description | Protein crystallography and calorimetry were used to characterize the binding of 1,2-azaborines to model cavities in T4 lysozyme in direct comparison to their carbonaceous counterparts. In the apolar L99A cavity, affinity for Ab dropped only slightly versus benzene. In the cavity designed to accommodate a single hydrogen bond (L99A/M102Q), Gln102O···HN hydrogen bonding for Ab and BEtAb was observed in the crystallographic complexes. The strength of the hydrogen bonding was estimated as 0.94 and 0.64 kcal/mol for Ab and BEtAb, respectively. This work unambiguously demonstrates that 1,2-azaborines can be readily accommodated in classic aryl recognition pockets and establishes one of 1,2-azaborine’s distinguishing features from its carbonaceous isostere benzene: its ability to serve as an NH hydrogen bond donor in a biological setting. |
doi_str_mv | 10.1021/jacs.6b06566 |
format | Article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5087281</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1822469757</sourcerecordid><originalsourceid>FETCH-LOGICAL-a417t-92e5441618421d36ba8661a424582914bcfd3db21872a3129a2ba0e130624c103</originalsourceid><addsrcrecordid>eNptkUFPGzEQRq2qVQnQG2fkYw8s9cx6vZsekCAqUClVD6Rna3bXSRxlbbC9SMuv70YJtJV6Glnz5s3IH2NnIC5BIHzZUBMvVS1UodQ7NoECRVYAqvdsIoTArKxUfsSOY9yMT4kVfGRHWCqRA6gJc_dDG_zKOH7jXWvdivslhwvMrl-o9sE6E7l1PK0Nv7F7YEbPNg07biH5fIj-ZegM_9Encil-5Q8p9E3qwzhIruWLtQmdbwdHnW3iKfuwpG00nw71hP26_baY3Wfzn3ffZ9fzjCSUKZuiKaQEBZVEaHNVU6UUkERZVDgFWTfLNm9rhKpEygGnhDUJA7lQKBsQ-Qm72nsf-7ozbWNcCrTVj8F2FAbtyep_O86u9co_60KMygpGweeDIPin3sSkOxsbs92SM76PGipEqaZlUY7oxR5tgo8xmOXbGhB6F5HeRaQPEY34-d-nvcGvmfxZvZva-D648af-7_oNIGOZ_A</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1822469757</pqid></control><display><type>article</type><title>Hydrogen Bonding of 1,2-Azaborines in the Binding Cavity of T4 Lysozyme Mutants: Structures and Thermodynamics</title><source>MEDLINE</source><source>American Chemical Society Journals</source><creator>Lee, Hyelee ; Fischer, Marcus ; Shoichet, Brian K ; Liu, Shih-Yuan</creator><creatorcontrib>Lee, Hyelee ; Fischer, Marcus ; Shoichet, Brian K ; Liu, Shih-Yuan</creatorcontrib><description>Protein crystallography and calorimetry were used to characterize the binding of 1,2-azaborines to model cavities in T4 lysozyme in direct comparison to their carbonaceous counterparts. In the apolar L99A cavity, affinity for Ab dropped only slightly versus benzene. In the cavity designed to accommodate a single hydrogen bond (L99A/M102Q), Gln102O···HN hydrogen bonding for Ab and BEtAb was observed in the crystallographic complexes. The strength of the hydrogen bonding was estimated as 0.94 and 0.64 kcal/mol for Ab and BEtAb, respectively. This work unambiguously demonstrates that 1,2-azaborines can be readily accommodated in classic aryl recognition pockets and establishes one of 1,2-azaborine’s distinguishing features from its carbonaceous isostere benzene: its ability to serve as an NH hydrogen bond donor in a biological setting.</description><identifier>ISSN: 0002-7863</identifier><identifier>EISSN: 1520-5126</identifier><identifier>DOI: 10.1021/jacs.6b06566</identifier><identifier>PMID: 27603116</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Boron Compounds - chemistry ; Calorimetry ; Hydrogen Bonding ; Models, Molecular ; Molecular Structure ; Muramidase - chemistry ; Muramidase - metabolism ; Thermodynamics</subject><ispartof>Journal of the American Chemical Society, 2016-09, Vol.138 (37), p.12021-12024</ispartof><rights>Copyright © 2016 American Chemical Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a417t-92e5441618421d36ba8661a424582914bcfd3db21872a3129a2ba0e130624c103</citedby><cites>FETCH-LOGICAL-a417t-92e5441618421d36ba8661a424582914bcfd3db21872a3129a2ba0e130624c103</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/jacs.6b06566$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jacs.6b06566$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>230,314,780,784,885,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27603116$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lee, Hyelee</creatorcontrib><creatorcontrib>Fischer, Marcus</creatorcontrib><creatorcontrib>Shoichet, Brian K</creatorcontrib><creatorcontrib>Liu, Shih-Yuan</creatorcontrib><title>Hydrogen Bonding of 1,2-Azaborines in the Binding Cavity of T4 Lysozyme Mutants: Structures and Thermodynamics</title><title>Journal of the American Chemical Society</title><addtitle>J. Am. Chem. Soc</addtitle><description>Protein crystallography and calorimetry were used to characterize the binding of 1,2-azaborines to model cavities in T4 lysozyme in direct comparison to their carbonaceous counterparts. In the apolar L99A cavity, affinity for Ab dropped only slightly versus benzene. In the cavity designed to accommodate a single hydrogen bond (L99A/M102Q), Gln102O···HN hydrogen bonding for Ab and BEtAb was observed in the crystallographic complexes. The strength of the hydrogen bonding was estimated as 0.94 and 0.64 kcal/mol for Ab and BEtAb, respectively. This work unambiguously demonstrates that 1,2-azaborines can be readily accommodated in classic aryl recognition pockets and establishes one of 1,2-azaborine’s distinguishing features from its carbonaceous isostere benzene: its ability to serve as an NH hydrogen bond donor in a biological setting.</description><subject>Boron Compounds - chemistry</subject><subject>Calorimetry</subject><subject>Hydrogen Bonding</subject><subject>Models, Molecular</subject><subject>Molecular Structure</subject><subject>Muramidase - chemistry</subject><subject>Muramidase - metabolism</subject><subject>Thermodynamics</subject><issn>0002-7863</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkUFPGzEQRq2qVQnQG2fkYw8s9cx6vZsekCAqUClVD6Rna3bXSRxlbbC9SMuv70YJtJV6Glnz5s3IH2NnIC5BIHzZUBMvVS1UodQ7NoECRVYAqvdsIoTArKxUfsSOY9yMT4kVfGRHWCqRA6gJc_dDG_zKOH7jXWvdivslhwvMrl-o9sE6E7l1PK0Nv7F7YEbPNg07biH5fIj-ZegM_9Encil-5Q8p9E3qwzhIruWLtQmdbwdHnW3iKfuwpG00nw71hP26_baY3Wfzn3ffZ9fzjCSUKZuiKaQEBZVEaHNVU6UUkERZVDgFWTfLNm9rhKpEygGnhDUJA7lQKBsQ-Qm72nsf-7ozbWNcCrTVj8F2FAbtyep_O86u9co_60KMygpGweeDIPin3sSkOxsbs92SM76PGipEqaZlUY7oxR5tgo8xmOXbGhB6F5HeRaQPEY34-d-nvcGvmfxZvZva-D648af-7_oNIGOZ_A</recordid><startdate>20160921</startdate><enddate>20160921</enddate><creator>Lee, Hyelee</creator><creator>Fischer, Marcus</creator><creator>Shoichet, Brian K</creator><creator>Liu, Shih-Yuan</creator><general>American Chemical Society</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20160921</creationdate><title>Hydrogen Bonding of 1,2-Azaborines in the Binding Cavity of T4 Lysozyme Mutants: Structures and Thermodynamics</title><author>Lee, Hyelee ; Fischer, Marcus ; Shoichet, Brian K ; Liu, Shih-Yuan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a417t-92e5441618421d36ba8661a424582914bcfd3db21872a3129a2ba0e130624c103</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Boron Compounds - chemistry</topic><topic>Calorimetry</topic><topic>Hydrogen Bonding</topic><topic>Models, Molecular</topic><topic>Molecular Structure</topic><topic>Muramidase - chemistry</topic><topic>Muramidase - metabolism</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lee, Hyelee</creatorcontrib><creatorcontrib>Fischer, Marcus</creatorcontrib><creatorcontrib>Shoichet, Brian K</creatorcontrib><creatorcontrib>Liu, Shih-Yuan</creatorcontrib><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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lee, Hyelee</au><au>Fischer, Marcus</au><au>Shoichet, Brian K</au><au>Liu, Shih-Yuan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Hydrogen Bonding of 1,2-Azaborines in the Binding Cavity of T4 Lysozyme Mutants: Structures and Thermodynamics</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>2016-09-21</date><risdate>2016</risdate><volume>138</volume><issue>37</issue><spage>12021</spage><epage>12024</epage><pages>12021-12024</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><abstract>Protein crystallography and calorimetry were used to characterize the binding of 1,2-azaborines to model cavities in T4 lysozyme in direct comparison to their carbonaceous counterparts. In the apolar L99A cavity, affinity for Ab dropped only slightly versus benzene. In the cavity designed to accommodate a single hydrogen bond (L99A/M102Q), Gln102O···HN hydrogen bonding for Ab and BEtAb was observed in the crystallographic complexes. The strength of the hydrogen bonding was estimated as 0.94 and 0.64 kcal/mol for Ab and BEtAb, respectively. This work unambiguously demonstrates that 1,2-azaborines can be readily accommodated in classic aryl recognition pockets and establishes one of 1,2-azaborine’s distinguishing features from its carbonaceous isostere benzene: its ability to serve as an NH hydrogen bond donor in a biological setting.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>27603116</pmid><doi>10.1021/jacs.6b06566</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0002-7863 |
ispartof | Journal of the American Chemical Society, 2016-09, Vol.138 (37), p.12021-12024 |
issn | 0002-7863 1520-5126 |
language | eng |
recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5087281 |
source | MEDLINE; American Chemical Society Journals |
subjects | Boron Compounds - chemistry Calorimetry Hydrogen Bonding Models, Molecular Molecular Structure Muramidase - chemistry Muramidase - metabolism Thermodynamics |
title | Hydrogen Bonding of 1,2-Azaborines in the Binding Cavity of T4 Lysozyme Mutants: Structures and Thermodynamics |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-27T16%3A36%3A20IST&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=Hydrogen%20Bonding%20of%201,2-Azaborines%20in%20the%20Binding%20Cavity%20of%20T4%20Lysozyme%20Mutants:%20Structures%20and%20Thermodynamics&rft.jtitle=Journal%20of%20the%20American%20Chemical%20Society&rft.au=Lee,%20Hyelee&rft.date=2016-09-21&rft.volume=138&rft.issue=37&rft.spage=12021&rft.epage=12024&rft.pages=12021-12024&rft.issn=0002-7863&rft.eissn=1520-5126&rft_id=info:doi/10.1021/jacs.6b06566&rft_dat=%3Cproquest_pubme%3E1822469757%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=1822469757&rft_id=info:pmid/27603116&rfr_iscdi=true |