Exploring the Strength of the H-Bond in Synthetic Models for Heme Proteins: The Importance of the N−H Acidity of the Distal Base
The distal hydrogen bond (H‐bond) in dioxygen‐binding proteins is crucial for the discrimination of O2 with respect to CO or NO. We report the preparation and characterization of a series of ZnII porphyrins, with one of three meso‐phenyl rings bearing both an alkyl‐tethered proximal imidazole ligand...
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| Veröffentlicht in: | Chemistry : a European journal 2016-07, Vol.22 (29), p.10194-10202 |
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| creator | Alberti, Mariza N. Polyhach, Yevhen Tzirakis, Manolis D. Tödtli, Laura Jeschke, Gunnar Diederich, François |
| description | The distal hydrogen bond (H‐bond) in dioxygen‐binding proteins is crucial for the discrimination of O2 with respect to CO or NO. We report the preparation and characterization of a series of ZnII porphyrins, with one of three meso‐phenyl rings bearing both an alkyl‐tethered proximal imidazole ligand and a heterocyclic distal H‐bond donor connected by a rigid acetylene spacer. Previously, we had validated the corresponding CoII complexes as synthetic model systems for dioxygen‐binding heme proteins and demonstrated the structural requirements for proper distal H‐bonding to CoII‐bound dioxygen. Here, we systematically vary the H‐bond donor ability of the distal heterocycles, as predicted based on pKa values. The H‐bond in the dioxygen adducts of the CoII porphyrins was directly measured by Q‐band Davies‐ENDOR spectroscopy. It was shown that the strength of the hyperfine coupling between the dioxygen radical and the distal H‐atom increases with enhanced acidity of the H‐bond donor.
The distal hydrogen bond in dioxygen‐binding proteins is crucial for the discrimination of O2 with respect to CO or NO. The H‐bond donor ability of distal heterocycles, as predicted based on pKa values, has been varied systematically. The H‐bond in the dioxygen adducts of the CoII porphyrins was directly measured by Q‐band Davies‐ENDOR spectroscopy, and it was shown that the strength of the hyperfine coupling between the dioxygen radical and the distal H‐atom increases with enhanced acidity of the H‐bond donor. |
| doi_str_mv | 10.1002/chem.201601505 |
| format | Article |
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The distal hydrogen bond in dioxygen‐binding proteins is crucial for the discrimination of O2 with respect to CO or NO. The H‐bond donor ability of distal heterocycles, as predicted based on pKa values, has been varied systematically. The H‐bond in the dioxygen adducts of the CoII porphyrins was directly measured by Q‐band Davies‐ENDOR spectroscopy, and it was shown that the strength of the hyperfine coupling between the dioxygen radical and the distal H‐atom increases with enhanced acidity of the H‐bond donor.</description><identifier>ISSN: 0947-6539</identifier><identifier>EISSN: 1521-3765</identifier><identifier>DOI: 10.1002/chem.201601505</identifier><identifier>PMID: 27312695</identifier><identifier>CODEN: CEUJED</identifier><language>eng</language><publisher>Germany: Blackwell Publishing Ltd</publisher><subject>Acetylene ; Acidity ; Adducts ; Binding ; Carrier Proteins - chemistry ; Chemistry ; Coupling ; dioxygen binding ; Discrimination ; ENDOR spectroscopy ; Heme proteins ; Hemeproteins - chemistry ; hydrogen bond ; Hydrogen Bonding ; Hydrogen bonds ; Imidazole ; Ligands ; model systems ; Models, Molecular ; NMR spectroscopy ; Oxygen - chemistry ; Porphyrins ; Porphyrins - chemistry ; Proteins ; Radicals ; Spectroscopic analysis ; Spectroscopy ; Spectrum Analysis ; Strength</subject><ispartof>Chemistry : a European journal, 2016-07, Vol.22 (29), p.10194-10202</ispartof><rights>2016 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><rights>2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.</rights><rights>2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5095-7f89a8c96cbca6aef348052ef8645e0b5249603ee4a9fbc73b28b89ad14bc803</citedby><cites>FETCH-LOGICAL-c5095-7f89a8c96cbca6aef348052ef8645e0b5249603ee4a9fbc73b28b89ad14bc803</cites><orcidid>0000-0001-6853-8585 ; 0000-0002-6009-1077 ; 0000-0002-8591-2038</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fchem.201601505$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fchem.201601505$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27312695$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Alberti, Mariza N.</creatorcontrib><creatorcontrib>Polyhach, Yevhen</creatorcontrib><creatorcontrib>Tzirakis, Manolis D.</creatorcontrib><creatorcontrib>Tödtli, Laura</creatorcontrib><creatorcontrib>Jeschke, Gunnar</creatorcontrib><creatorcontrib>Diederich, François</creatorcontrib><title>Exploring the Strength of the H-Bond in Synthetic Models for Heme Proteins: The Importance of the N−H Acidity of the Distal Base</title><title>Chemistry : a European journal</title><addtitle>Chem. Eur. J</addtitle><description>The distal hydrogen bond (H‐bond) in dioxygen‐binding proteins is crucial for the discrimination of O2 with respect to CO or NO. We report the preparation and characterization of a series of ZnII porphyrins, with one of three meso‐phenyl rings bearing both an alkyl‐tethered proximal imidazole ligand and a heterocyclic distal H‐bond donor connected by a rigid acetylene spacer. Previously, we had validated the corresponding CoII complexes as synthetic model systems for dioxygen‐binding heme proteins and demonstrated the structural requirements for proper distal H‐bonding to CoII‐bound dioxygen. Here, we systematically vary the H‐bond donor ability of the distal heterocycles, as predicted based on pKa values. The H‐bond in the dioxygen adducts of the CoII porphyrins was directly measured by Q‐band Davies‐ENDOR spectroscopy. It was shown that the strength of the hyperfine coupling between the dioxygen radical and the distal H‐atom increases with enhanced acidity of the H‐bond donor.
The distal hydrogen bond in dioxygen‐binding proteins is crucial for the discrimination of O2 with respect to CO or NO. The H‐bond donor ability of distal heterocycles, as predicted based on pKa values, has been varied systematically. The H‐bond in the dioxygen adducts of the CoII porphyrins was directly measured by Q‐band Davies‐ENDOR spectroscopy, and it was shown that the strength of the hyperfine coupling between the dioxygen radical and the distal H‐atom increases with enhanced acidity of the H‐bond donor.</description><subject>Acetylene</subject><subject>Acidity</subject><subject>Adducts</subject><subject>Binding</subject><subject>Carrier Proteins - chemistry</subject><subject>Chemistry</subject><subject>Coupling</subject><subject>dioxygen binding</subject><subject>Discrimination</subject><subject>ENDOR spectroscopy</subject><subject>Heme proteins</subject><subject>Hemeproteins - chemistry</subject><subject>hydrogen bond</subject><subject>Hydrogen Bonding</subject><subject>Hydrogen bonds</subject><subject>Imidazole</subject><subject>Ligands</subject><subject>model systems</subject><subject>Models, Molecular</subject><subject>NMR spectroscopy</subject><subject>Oxygen - chemistry</subject><subject>Porphyrins</subject><subject>Porphyrins - chemistry</subject><subject>Proteins</subject><subject>Radicals</subject><subject>Spectroscopic analysis</subject><subject>Spectroscopy</subject><subject>Spectrum Analysis</subject><subject>Strength</subject><issn>0947-6539</issn><issn>1521-3765</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU1v00AQhi0EoqFw5YhW4sLFYT-8X9yakNaV0gKqBcfVejNuXGxv2HXU5sqJMz-RX4JDmghxAE6jGT3vK42eJHlO8JhgTF-7JbRjionAhGP-IBkRTknKpOAPkxHWmUwFZ_ooeRLjDcZYC8YeJ0dUMkKF5qPk6-xu1fhQd9eoXwK66gN01_0S-erXnqcT3y1Q3aGrTTcc-tqhC7-AJqLKB5RDC-h98D3UXXyDiiFx3q586G3nYN9x-ePb9xyduHpR95v98W0de9ugiY3wNHlU2SbCs_t5nBSns2Kap_N3Z-fTk3nqONY8lZXSVjktXOmssFCxTGFOoVIi44BLTjMtMAPIrK5KJ1lJVTlEFiQrncLsOHm1q10F_2UNsTdtHR00je3Ar6MhinKeSYnVf6CYZlJkYou-_AO98evQDX8YoqnkVGCl_0opTKTSg46BGu8oF3yMASqzCnVrw8YQbLa2zda2OdgeAi_ua9dlC4sDvtc7AHoH3NYNbP5RZ6b57OL38nSXHUzB3SFrw2cjJJPcfLo8MwX7WEzY_IMh7CcTRMPr</recordid><startdate>20160711</startdate><enddate>20160711</enddate><creator>Alberti, Mariza N.</creator><creator>Polyhach, Yevhen</creator><creator>Tzirakis, Manolis D.</creator><creator>Tödtli, Laura</creator><creator>Jeschke, Gunnar</creator><creator>Diederich, François</creator><general>Blackwell Publishing Ltd</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</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>7SR</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>K9.</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0001-6853-8585</orcidid><orcidid>https://orcid.org/0000-0002-6009-1077</orcidid><orcidid>https://orcid.org/0000-0002-8591-2038</orcidid></search><sort><creationdate>20160711</creationdate><title>Exploring the Strength of the H-Bond in Synthetic Models for Heme Proteins: The Importance of the N−H Acidity of the Distal Base</title><author>Alberti, Mariza N. ; Polyhach, Yevhen ; Tzirakis, Manolis D. ; Tödtli, Laura ; Jeschke, Gunnar ; Diederich, François</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5095-7f89a8c96cbca6aef348052ef8645e0b5249603ee4a9fbc73b28b89ad14bc803</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Acetylene</topic><topic>Acidity</topic><topic>Adducts</topic><topic>Binding</topic><topic>Carrier Proteins - chemistry</topic><topic>Chemistry</topic><topic>Coupling</topic><topic>dioxygen binding</topic><topic>Discrimination</topic><topic>ENDOR spectroscopy</topic><topic>Heme proteins</topic><topic>Hemeproteins - chemistry</topic><topic>hydrogen bond</topic><topic>Hydrogen Bonding</topic><topic>Hydrogen bonds</topic><topic>Imidazole</topic><topic>Ligands</topic><topic>model systems</topic><topic>Models, Molecular</topic><topic>NMR spectroscopy</topic><topic>Oxygen - chemistry</topic><topic>Porphyrins</topic><topic>Porphyrins - chemistry</topic><topic>Proteins</topic><topic>Radicals</topic><topic>Spectroscopic analysis</topic><topic>Spectroscopy</topic><topic>Spectrum Analysis</topic><topic>Strength</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Alberti, Mariza N.</creatorcontrib><creatorcontrib>Polyhach, Yevhen</creatorcontrib><creatorcontrib>Tzirakis, Manolis D.</creatorcontrib><creatorcontrib>Tödtli, Laura</creatorcontrib><creatorcontrib>Jeschke, Gunnar</creatorcontrib><creatorcontrib>Diederich, François</creatorcontrib><collection>Istex</collection><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>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>MEDLINE - Academic</collection><jtitle>Chemistry : a European journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Alberti, Mariza N.</au><au>Polyhach, Yevhen</au><au>Tzirakis, Manolis D.</au><au>Tödtli, Laura</au><au>Jeschke, Gunnar</au><au>Diederich, François</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Exploring the Strength of the H-Bond in Synthetic Models for Heme Proteins: The Importance of the N−H Acidity of the Distal Base</atitle><jtitle>Chemistry : a European journal</jtitle><addtitle>Chem. Eur. J</addtitle><date>2016-07-11</date><risdate>2016</risdate><volume>22</volume><issue>29</issue><spage>10194</spage><epage>10202</epage><pages>10194-10202</pages><issn>0947-6539</issn><eissn>1521-3765</eissn><coden>CEUJED</coden><abstract>The distal hydrogen bond (H‐bond) in dioxygen‐binding proteins is crucial for the discrimination of O2 with respect to CO or NO. We report the preparation and characterization of a series of ZnII porphyrins, with one of three meso‐phenyl rings bearing both an alkyl‐tethered proximal imidazole ligand and a heterocyclic distal H‐bond donor connected by a rigid acetylene spacer. Previously, we had validated the corresponding CoII complexes as synthetic model systems for dioxygen‐binding heme proteins and demonstrated the structural requirements for proper distal H‐bonding to CoII‐bound dioxygen. Here, we systematically vary the H‐bond donor ability of the distal heterocycles, as predicted based on pKa values. The H‐bond in the dioxygen adducts of the CoII porphyrins was directly measured by Q‐band Davies‐ENDOR spectroscopy. It was shown that the strength of the hyperfine coupling between the dioxygen radical and the distal H‐atom increases with enhanced acidity of the H‐bond donor.
The distal hydrogen bond in dioxygen‐binding proteins is crucial for the discrimination of O2 with respect to CO or NO. The H‐bond donor ability of distal heterocycles, as predicted based on pKa values, has been varied systematically. The H‐bond in the dioxygen adducts of the CoII porphyrins was directly measured by Q‐band Davies‐ENDOR spectroscopy, and it was shown that the strength of the hyperfine coupling between the dioxygen radical and the distal H‐atom increases with enhanced acidity of the H‐bond donor.</abstract><cop>Germany</cop><pub>Blackwell Publishing Ltd</pub><pmid>27312695</pmid><doi>10.1002/chem.201601505</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0001-6853-8585</orcidid><orcidid>https://orcid.org/0000-0002-6009-1077</orcidid><orcidid>https://orcid.org/0000-0002-8591-2038</orcidid></addata></record> |
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| subjects | Acetylene Acidity Adducts Binding Carrier Proteins - chemistry Chemistry Coupling dioxygen binding Discrimination ENDOR spectroscopy Heme proteins Hemeproteins - chemistry hydrogen bond Hydrogen Bonding Hydrogen bonds Imidazole Ligands model systems Models, Molecular NMR spectroscopy Oxygen - chemistry Porphyrins Porphyrins - chemistry Proteins Radicals Spectroscopic analysis Spectroscopy Spectrum Analysis Strength |
| title | Exploring the Strength of the H-Bond in Synthetic Models for Heme Proteins: The Importance of the N−H Acidity of the Distal Base |
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