Reconstitution of Heme Enzymes with Artificial Metalloporphyrinoids
An important strategy used in engineering of hemoproteins to generate artificial enzymes involves replacement of heme with an artificial cofactor after removal of the native heme cofactor under acidic conditions. Replacement of heme in an enzyme with a nonnatural metalloporphyrinoid can significantl...
Gespeichert in:
| Veröffentlicht in: | Methods in enzymology 2016, Vol.580, p.439-454 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 454 |
|---|---|
| container_issue | |
| container_start_page | 439 |
| container_title | Methods in enzymology |
| container_volume | 580 |
| creator | Oohora, K Hayashi, T |
| description | An important strategy used in engineering of hemoproteins to generate artificial enzymes involves replacement of heme with an artificial cofactor after removal of the native heme cofactor under acidic conditions. Replacement of heme in an enzyme with a nonnatural metalloporphyrinoid can significantly alter the reactivity of the enzyme. This chapter describes the design and synthesis of three types of artificial metalloporphyrinoid cofactors consisting of mono-, di-, and tri-anionic ligands (tetradehydrocorrin, porphycene, and corrole, respectively). In addition, practical procedures for the preparation of apo-hemoproteins, incorporation of artificial cofactors, and characterization techniques are presented. Furthermore, the representative catalytic activities of artificial enzymes generated by reconstitution of hemoproteins are summarized. |
| doi_str_mv | 10.1016/bs.mie.2016.05.049 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_1816632856</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1816632856</sourcerecordid><originalsourceid>FETCH-LOGICAL-c260t-e64954c842bf8a6a242fac1f91b699ec146d5bfe2e55f339e5acac98897e2b83</originalsourceid><addsrcrecordid>eNo1j8FLwzAchYMgbk7_AQ_So5fWJE3S5DjK3ISJILuXNP2FRdqmNilS_3oLztN7h4-P9xB6IDgjmIjnOmSdg4wuPcM8w0xdoTXhvEgLJeUK3YbwiTEtpCI3aEULLkXO2BqVH2B8H6KLU3S-T7xNDtBBsut_5g5C8u3iOdmO0VlnnG6TN4i6bf3gx-E8j673rgl36NrqNsD9JTfo9LI7lYf0-L5_LbfH1FCBYwqCKc6MZLS2UgtNGbXaEKtILZQCQ5hoeG2BAuc2zxVwbbRZ1qsCaC3zDXr60w6j_5ogxKpzwUDb6h78FCoiiRA5lVws6OMFneoOmmoYXafHufr_nf8CQOJagw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1816632856</pqid></control><display><type>article</type><title>Reconstitution of Heme Enzymes with Artificial Metalloporphyrinoids</title><source>MEDLINE</source><source>ScienceDirect Journals (5 years ago - present)</source><creator>Oohora, K ; Hayashi, T</creator><creatorcontrib>Oohora, K ; Hayashi, T</creatorcontrib><description>An important strategy used in engineering of hemoproteins to generate artificial enzymes involves replacement of heme with an artificial cofactor after removal of the native heme cofactor under acidic conditions. Replacement of heme in an enzyme with a nonnatural metalloporphyrinoid can significantly alter the reactivity of the enzyme. This chapter describes the design and synthesis of three types of artificial metalloporphyrinoid cofactors consisting of mono-, di-, and tri-anionic ligands (tetradehydrocorrin, porphycene, and corrole, respectively). In addition, practical procedures for the preparation of apo-hemoproteins, incorporation of artificial cofactors, and characterization techniques are presented. Furthermore, the representative catalytic activities of artificial enzymes generated by reconstitution of hemoproteins are summarized.</description><identifier>EISSN: 1557-7988</identifier><identifier>DOI: 10.1016/bs.mie.2016.05.049</identifier><identifier>PMID: 27586344</identifier><language>eng</language><publisher>United States</publisher><subject>Corrinoids - chemical synthesis ; Corrinoids - chemistry ; Heme - chemistry ; Hemeproteins - chemical synthesis ; Hemeproteins - chemistry ; Kinetics ; Metalloporphyrins - chemical synthesis ; Metalloporphyrins - chemistry ; Porphyrins - chemical synthesis ; Porphyrins - chemistry ; Protein Engineering - methods</subject><ispartof>Methods in enzymology, 2016, Vol.580, p.439-454</ispartof><rights>2016 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c260t-e64954c842bf8a6a242fac1f91b699ec146d5bfe2e55f339e5acac98897e2b83</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,4023,27922,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27586344$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Oohora, K</creatorcontrib><creatorcontrib>Hayashi, T</creatorcontrib><title>Reconstitution of Heme Enzymes with Artificial Metalloporphyrinoids</title><title>Methods in enzymology</title><addtitle>Methods Enzymol</addtitle><description>An important strategy used in engineering of hemoproteins to generate artificial enzymes involves replacement of heme with an artificial cofactor after removal of the native heme cofactor under acidic conditions. Replacement of heme in an enzyme with a nonnatural metalloporphyrinoid can significantly alter the reactivity of the enzyme. This chapter describes the design and synthesis of three types of artificial metalloporphyrinoid cofactors consisting of mono-, di-, and tri-anionic ligands (tetradehydrocorrin, porphycene, and corrole, respectively). In addition, practical procedures for the preparation of apo-hemoproteins, incorporation of artificial cofactors, and characterization techniques are presented. Furthermore, the representative catalytic activities of artificial enzymes generated by reconstitution of hemoproteins are summarized.</description><subject>Corrinoids - chemical synthesis</subject><subject>Corrinoids - chemistry</subject><subject>Heme - chemistry</subject><subject>Hemeproteins - chemical synthesis</subject><subject>Hemeproteins - chemistry</subject><subject>Kinetics</subject><subject>Metalloporphyrins - chemical synthesis</subject><subject>Metalloporphyrins - chemistry</subject><subject>Porphyrins - chemical synthesis</subject><subject>Porphyrins - chemistry</subject><subject>Protein Engineering - methods</subject><issn>1557-7988</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo1j8FLwzAchYMgbk7_AQ_So5fWJE3S5DjK3ISJILuXNP2FRdqmNilS_3oLztN7h4-P9xB6IDgjmIjnOmSdg4wuPcM8w0xdoTXhvEgLJeUK3YbwiTEtpCI3aEULLkXO2BqVH2B8H6KLU3S-T7xNDtBBsut_5g5C8u3iOdmO0VlnnG6TN4i6bf3gx-E8j673rgl36NrqNsD9JTfo9LI7lYf0-L5_LbfH1FCBYwqCKc6MZLS2UgtNGbXaEKtILZQCQ5hoeG2BAuc2zxVwbbRZ1qsCaC3zDXr60w6j_5ogxKpzwUDb6h78FCoiiRA5lVws6OMFneoOmmoYXafHufr_nf8CQOJagw</recordid><startdate>2016</startdate><enddate>2016</enddate><creator>Oohora, K</creator><creator>Hayashi, T</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>2016</creationdate><title>Reconstitution of Heme Enzymes with Artificial Metalloporphyrinoids</title><author>Oohora, K ; Hayashi, T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c260t-e64954c842bf8a6a242fac1f91b699ec146d5bfe2e55f339e5acac98897e2b83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Corrinoids - chemical synthesis</topic><topic>Corrinoids - chemistry</topic><topic>Heme - chemistry</topic><topic>Hemeproteins - chemical synthesis</topic><topic>Hemeproteins - chemistry</topic><topic>Kinetics</topic><topic>Metalloporphyrins - chemical synthesis</topic><topic>Metalloporphyrins - chemistry</topic><topic>Porphyrins - chemical synthesis</topic><topic>Porphyrins - chemistry</topic><topic>Protein Engineering - methods</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Oohora, K</creatorcontrib><creatorcontrib>Hayashi, T</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Methods in enzymology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Oohora, K</au><au>Hayashi, T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Reconstitution of Heme Enzymes with Artificial Metalloporphyrinoids</atitle><jtitle>Methods in enzymology</jtitle><addtitle>Methods Enzymol</addtitle><date>2016</date><risdate>2016</risdate><volume>580</volume><spage>439</spage><epage>454</epage><pages>439-454</pages><eissn>1557-7988</eissn><abstract>An important strategy used in engineering of hemoproteins to generate artificial enzymes involves replacement of heme with an artificial cofactor after removal of the native heme cofactor under acidic conditions. Replacement of heme in an enzyme with a nonnatural metalloporphyrinoid can significantly alter the reactivity of the enzyme. This chapter describes the design and synthesis of three types of artificial metalloporphyrinoid cofactors consisting of mono-, di-, and tri-anionic ligands (tetradehydrocorrin, porphycene, and corrole, respectively). In addition, practical procedures for the preparation of apo-hemoproteins, incorporation of artificial cofactors, and characterization techniques are presented. Furthermore, the representative catalytic activities of artificial enzymes generated by reconstitution of hemoproteins are summarized.</abstract><cop>United States</cop><pmid>27586344</pmid><doi>10.1016/bs.mie.2016.05.049</doi><tpages>16</tpages></addata></record> |
| fulltext | fulltext |
| identifier | EISSN: 1557-7988 |
| ispartof | Methods in enzymology, 2016, Vol.580, p.439-454 |
| issn | 1557-7988 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1816632856 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Corrinoids - chemical synthesis Corrinoids - chemistry Heme - chemistry Hemeproteins - chemical synthesis Hemeproteins - chemistry Kinetics Metalloporphyrins - chemical synthesis Metalloporphyrins - chemistry Porphyrins - chemical synthesis Porphyrins - chemistry Protein Engineering - methods |
| title | Reconstitution of Heme Enzymes with Artificial Metalloporphyrinoids |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-08T09%3A29%3A01IST&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=Reconstitution%20of%20Heme%20Enzymes%20with%20Artificial%20Metalloporphyrinoids&rft.jtitle=Methods%20in%20enzymology&rft.au=Oohora,%20K&rft.date=2016&rft.volume=580&rft.spage=439&rft.epage=454&rft.pages=439-454&rft.eissn=1557-7988&rft_id=info:doi/10.1016/bs.mie.2016.05.049&rft_dat=%3Cproquest_pubme%3E1816632856%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=1816632856&rft_id=info:pmid/27586344&rfr_iscdi=true |