Histidine orientation in artificial peroxidase regioisomers as determined by paramagnetic NMR shifts
Fe-Mimochrome VI*a is a synthetic peroxidase and peroxygenase, featuring two different peptides that are covalently-linked to deuteroheme. To perform a systematic structure/function correlation, we purposely shortened the distance between the distal peptide and the heme, allowing for the separation...
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| Veröffentlicht in: | Chemical communications (Cambridge, England) England), 2021-02, Vol.57 (8), p.99-993 |
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| creator | Maglio, Ornella Chino, Marco Vicari, Claudia Pavone, Vincenzo Louro, Ricardo O Lombardi, Angela |
| description | Fe-Mimochrome VI*a is a synthetic peroxidase and peroxygenase, featuring two different peptides that are covalently-linked to deuteroheme. To perform a systematic structure/function correlation, we purposely shortened the distance between the distal peptide and the heme, allowing for the separation and characterization of two regioisomers. They differ in both His axial-ligand orientation, as determined by paramagnetic NMR shifts, and activity. These findings highlight that synthetic metalloenzymes may provide an efficient tool for disentangling the role of axial ligand orientation over peroxidase activity.
A semi-empirical approach allows determining the His axial-ligand orientation with respect to the porphyrin plane in synthetic heme-peroxidases, for structure/function analysis. |
| doi_str_mv | 10.1039/d0cc06676a |
| format | Article |
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A semi-empirical approach allows determining the His axial-ligand orientation with respect to the porphyrin plane in synthetic heme-peroxidases, for structure/function analysis.</description><subject>Chemistry</subject><subject>Chemistry, Multidisciplinary</subject><subject>Histidine</subject><subject>Ligands</subject><subject>NMR</subject><subject>Nuclear magnetic resonance</subject><subject>Orientation</subject><subject>Peptides</subject><subject>Peroxidase</subject><subject>Physical Sciences</subject><subject>Science & Technology</subject><issn>1359-7345</issn><issn>1364-548X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>HGBXW</sourceid><recordid>eNqN0s9rFTEQB_AgFvtDL96VgBdRVpM3STZ7LGtthaogCt6WvGRSU95unkkW2__ePLd9gidzSQ6f7zDMhJCnnL3hDLq3jlnLlGqVeUCOOCjRSKG_P9y9Zde0IOQhOc75mtXDpX5EDgGg67iAI-IuQi7BhQlpTAGnYkqIEw0TNakEH2wwG7rFFG-CMxlpwqsQQ44jpkxNpg4LprHGHV3f0q1JZjRXE5Zg6aePX2j-EXzJj8mBN5uMT-7uE_Lt_dnX_qK5_Hz-oT-9bCxAW5pWOaV165zWiq3QSWZFa4zgWqHVAAi2XSvnBTIpQUoU0qHvOBiujfAeTsjLpe42xZ8z5jKMIVvcbMyEcc7DSrQSOr3SXaUv_qHXcU5T7a4qLVa1AcarerUom2LOCf2wTWE06XbgbNjNfnjH-v7P7E8rfn5Xcl6P6Pb0ftgVvF7AL1xHn20dt8U9q8tRHITifLcnWbX-f92HZXF9nKdSo8-WaMp2n_j7S-A3MASp7A</recordid><startdate>20210201</startdate><enddate>20210201</enddate><creator>Maglio, Ornella</creator><creator>Chino, Marco</creator><creator>Vicari, Claudia</creator><creator>Pavone, Vincenzo</creator><creator>Louro, Ricardo O</creator><creator>Lombardi, Angela</creator><general>Royal Soc Chemistry</general><general>Royal Society of Chemistry</general><scope>BLEPL</scope><scope>DTL</scope><scope>HGBXW</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><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-0436-3293</orcidid><orcidid>https://orcid.org/0000-0002-2013-3009</orcidid><orcidid>https://orcid.org/0000-0001-6432-0802</orcidid><orcidid>https://orcid.org/0000-0002-2392-6450</orcidid><orcidid>https://orcid.org/0000-0002-7829-1907</orcidid></search><sort><creationdate>20210201</creationdate><title>Histidine orientation in artificial peroxidase regioisomers as determined by paramagnetic NMR shifts</title><author>Maglio, Ornella ; Chino, Marco ; Vicari, Claudia ; Pavone, Vincenzo ; Louro, Ricardo O ; Lombardi, Angela</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c337t-76d6887dd88602ed50c47aa4186ec833e3c7b6df4e055355e45def913a18a4ff3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Chemistry</topic><topic>Chemistry, Multidisciplinary</topic><topic>Histidine</topic><topic>Ligands</topic><topic>NMR</topic><topic>Nuclear magnetic resonance</topic><topic>Orientation</topic><topic>Peptides</topic><topic>Peroxidase</topic><topic>Physical Sciences</topic><topic>Science & Technology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Maglio, Ornella</creatorcontrib><creatorcontrib>Chino, Marco</creatorcontrib><creatorcontrib>Vicari, Claudia</creatorcontrib><creatorcontrib>Pavone, Vincenzo</creatorcontrib><creatorcontrib>Louro, Ricardo O</creatorcontrib><creatorcontrib>Lombardi, Angela</creatorcontrib><collection>Web of Science Core Collection</collection><collection>Science Citation Index Expanded</collection><collection>Web of Science - Science Citation Index Expanded - 2021</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><collection>MEDLINE - Academic</collection><jtitle>Chemical communications (Cambridge, England)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Maglio, Ornella</au><au>Chino, Marco</au><au>Vicari, Claudia</au><au>Pavone, Vincenzo</au><au>Louro, Ricardo O</au><au>Lombardi, Angela</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Histidine orientation in artificial peroxidase regioisomers as determined by paramagnetic NMR shifts</atitle><jtitle>Chemical communications (Cambridge, England)</jtitle><stitle>CHEM COMMUN</stitle><addtitle>Chem Commun (Camb)</addtitle><date>2021-02-01</date><risdate>2021</risdate><volume>57</volume><issue>8</issue><spage>99</spage><epage>993</epage><pages>99-993</pages><issn>1359-7345</issn><eissn>1364-548X</eissn><abstract>Fe-Mimochrome VI*a is a synthetic peroxidase and peroxygenase, featuring two different peptides that are covalently-linked to deuteroheme. To perform a systematic structure/function correlation, we purposely shortened the distance between the distal peptide and the heme, allowing for the separation and characterization of two regioisomers. They differ in both His axial-ligand orientation, as determined by paramagnetic NMR shifts, and activity. These findings highlight that synthetic metalloenzymes may provide an efficient tool for disentangling the role of axial ligand orientation over peroxidase activity.
A semi-empirical approach allows determining the His axial-ligand orientation with respect to the porphyrin plane in synthetic heme-peroxidases, for structure/function analysis.</abstract><cop>CAMBRIDGE</cop><pub>Royal Soc Chemistry</pub><pmid>33399143</pmid><doi>10.1039/d0cc06676a</doi><orcidid>https://orcid.org/0000-0002-0436-3293</orcidid><orcidid>https://orcid.org/0000-0002-2013-3009</orcidid><orcidid>https://orcid.org/0000-0001-6432-0802</orcidid><orcidid>https://orcid.org/0000-0002-2392-6450</orcidid><orcidid>https://orcid.org/0000-0002-7829-1907</orcidid></addata></record> |
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| source | Royal Society Of Chemistry Journals; Web of Science - Science Citation Index Expanded - 2021<img src="https://exlibris-pub.s3.amazonaws.com/fromwos-v2.jpg" />; Alma/SFX Local Collection |
| subjects | Chemistry Chemistry, Multidisciplinary Histidine Ligands NMR Nuclear magnetic resonance Orientation Peptides Peroxidase Physical Sciences Science & Technology |
| title | Histidine orientation in artificial peroxidase regioisomers as determined by paramagnetic NMR shifts |
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