Interpretation of the reactivity of peroxidase compounds I and II with phenols by the Marcus equation
The catalytic cycle of heme peroxidases involves two reactive states, compound I and compound II. Although their reduction potentials at pH 7 are similar, compound I is in general more reactive towards organic substrates than compound II. The different reactivities have until now remained unexplaine...
Gespeichert in:
| Veröffentlicht in: | FEBS letters 1997-07, Vol.412 (2), p.305-308 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 308 |
|---|---|
| container_issue | 2 |
| container_start_page | 305 |
| container_title | FEBS letters |
| container_volume | 412 |
| creator | Folkes, Lisa K Candeias, Luis P |
| description | The catalytic cycle of heme peroxidases involves two reactive states, compound I and compound II. Although their reduction potentials at pH 7 are similar, compound I is in general more reactive towards organic substrates than compound II. The different reactivities have until now remained unexplained. In this study, the reactions of compounds I and II of peroxidase from horseradish with phenols were analyzed using the Marcus equation of electron-transfer. Both reactions exhibit similar reorganization energies, and the different reactivities of the two enzyme states can be ascribed to a higher apparent rate of activationless electron-transfer in the compound I reactions. This can be attributed to the shorter electron-tunneling distance on electron-transfer to the porphyrin radical cation in compound I, compared to electron-transfer to the iron ion in compound II. |
| doi_str_mv | 10.1016/S0014-5793(97)00792-8 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_79191838</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0014579397007928</els_id><sourcerecordid>79191838</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4258-938d46b1b727e6d47b90452bce0c73764bb8bb3b9a6db7dc688959e251591dcc3</originalsourceid><addsrcrecordid>eNqNkMtqGzEUhkVpcRy3jxDQKrSLaaS5SVqVxjjJgEsWaddCl2OsMh6NJU0Sv309Y5NtsxI6_-UcPoSuKPlOCa1vngihZVYxUXwV7BshTOQZ_4DmlLMiK8qaf0TzN8sFuozxLzn-ORUzNBN5VeclmSNougShD5BUcr7DfoPTFnAAZZJ7dukwTnoI_tVZFQEbv-v90NmIG6w6i5sGv7i0xf0WOt9GrA9T_pcKZogY9sNU-xl92qg2wpfzu0B_7la_lw_Z-vG-Wf5cZ6bMK56Jgtuy1lSznEFtS6YFKatcGyCGFawuteZaF1qo2mpmTc25qATkFa0EtcYUC3R96u2D3w8Qk9y5aKBtVQd-iJIJKigv-NFYnYwm-BgDbGQf3E6Fg6REjnjlhFeO7KRgcsIrx9zVecGgd2DfUmeeR_3hpL-4Fg7vK5V3q9t8UkZBsGk8rvpxqoIjsGcHQUbjoDNgXQCTpPXuP8f-A-HOnsA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>79191838</pqid></control><display><type>article</type><title>Interpretation of the reactivity of peroxidase compounds I and II with phenols by the Marcus equation</title><source>Wiley Free Content</source><source>MEDLINE</source><source>Wiley Online Library Journals Frontfile Complete</source><source>Elsevier ScienceDirect Journals</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Alma/SFX Local Collection</source><creator>Folkes, Lisa K ; Candeias, Luis P</creator><creatorcontrib>Folkes, Lisa K ; Candeias, Luis P</creatorcontrib><description>The catalytic cycle of heme peroxidases involves two reactive states, compound I and compound II. Although their reduction potentials at pH 7 are similar, compound I is in general more reactive towards organic substrates than compound II. The different reactivities have until now remained unexplained. In this study, the reactions of compounds I and II of peroxidase from horseradish with phenols were analyzed using the Marcus equation of electron-transfer. Both reactions exhibit similar reorganization energies, and the different reactivities of the two enzyme states can be ascribed to a higher apparent rate of activationless electron-transfer in the compound I reactions. This can be attributed to the shorter electron-tunneling distance on electron-transfer to the porphyrin radical cation in compound I, compared to electron-transfer to the iron ion in compound II.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(97)00792-8</identifier><identifier>PMID: 9256240</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Catalysis ; Electron-transfer ; Heme - chemistry ; Heme peroxidase ; Kinetics ; Marcus equation ; Peroxidases - chemistry ; Phenols - chemistry ; Phenoxyl radical ; Stopped-flow ; Substrate Specificity ; Thermodynamics</subject><ispartof>FEBS letters, 1997-07, Vol.412 (2), p.305-308</ispartof><rights>1997 Federation of European Biochemical Societies</rights><rights>FEBS Letters 412 (1997) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4258-938d46b1b727e6d47b90452bce0c73764bb8bb3b9a6db7dc688959e251591dcc3</citedby><cites>FETCH-LOGICAL-c4258-938d46b1b727e6d47b90452bce0c73764bb8bb3b9a6db7dc688959e251591dcc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2897%2900792-8$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579397007928$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3537,27901,27902,45550,45551,46384,46808,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9256240$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Folkes, Lisa K</creatorcontrib><creatorcontrib>Candeias, Luis P</creatorcontrib><title>Interpretation of the reactivity of peroxidase compounds I and II with phenols by the Marcus equation</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>The catalytic cycle of heme peroxidases involves two reactive states, compound I and compound II. Although their reduction potentials at pH 7 are similar, compound I is in general more reactive towards organic substrates than compound II. The different reactivities have until now remained unexplained. In this study, the reactions of compounds I and II of peroxidase from horseradish with phenols were analyzed using the Marcus equation of electron-transfer. Both reactions exhibit similar reorganization energies, and the different reactivities of the two enzyme states can be ascribed to a higher apparent rate of activationless electron-transfer in the compound I reactions. This can be attributed to the shorter electron-tunneling distance on electron-transfer to the porphyrin radical cation in compound I, compared to electron-transfer to the iron ion in compound II.</description><subject>Catalysis</subject><subject>Electron-transfer</subject><subject>Heme - chemistry</subject><subject>Heme peroxidase</subject><subject>Kinetics</subject><subject>Marcus equation</subject><subject>Peroxidases - chemistry</subject><subject>Phenols - chemistry</subject><subject>Phenoxyl radical</subject><subject>Stopped-flow</subject><subject>Substrate Specificity</subject><subject>Thermodynamics</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkMtqGzEUhkVpcRy3jxDQKrSLaaS5SVqVxjjJgEsWaddCl2OsMh6NJU0Sv309Y5NtsxI6_-UcPoSuKPlOCa1vngihZVYxUXwV7BshTOQZ_4DmlLMiK8qaf0TzN8sFuozxLzn-ORUzNBN5VeclmSNougShD5BUcr7DfoPTFnAAZZJ7dukwTnoI_tVZFQEbv-v90NmIG6w6i5sGv7i0xf0WOt9GrA9T_pcKZogY9sNU-xl92qg2wpfzu0B_7la_lw_Z-vG-Wf5cZ6bMK56Jgtuy1lSznEFtS6YFKatcGyCGFawuteZaF1qo2mpmTc25qATkFa0EtcYUC3R96u2D3w8Qk9y5aKBtVQd-iJIJKigv-NFYnYwm-BgDbGQf3E6Fg6REjnjlhFeO7KRgcsIrx9zVecGgd2DfUmeeR_3hpL-4Fg7vK5V3q9t8UkZBsGk8rvpxqoIjsGcHQUbjoDNgXQCTpPXuP8f-A-HOnsA</recordid><startdate>19970728</startdate><enddate>19970728</enddate><creator>Folkes, Lisa K</creator><creator>Candeias, Luis P</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>19970728</creationdate><title>Interpretation of the reactivity of peroxidase compounds I and II with phenols by the Marcus equation</title><author>Folkes, Lisa K ; Candeias, Luis P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4258-938d46b1b727e6d47b90452bce0c73764bb8bb3b9a6db7dc688959e251591dcc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Catalysis</topic><topic>Electron-transfer</topic><topic>Heme - chemistry</topic><topic>Heme peroxidase</topic><topic>Kinetics</topic><topic>Marcus equation</topic><topic>Peroxidases - chemistry</topic><topic>Phenols - chemistry</topic><topic>Phenoxyl radical</topic><topic>Stopped-flow</topic><topic>Substrate Specificity</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Folkes, Lisa K</creatorcontrib><creatorcontrib>Candeias, Luis P</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Folkes, Lisa K</au><au>Candeias, Luis P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interpretation of the reactivity of peroxidase compounds I and II with phenols by the Marcus equation</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1997-07-28</date><risdate>1997</risdate><volume>412</volume><issue>2</issue><spage>305</spage><epage>308</epage><pages>305-308</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>The catalytic cycle of heme peroxidases involves two reactive states, compound I and compound II. Although their reduction potentials at pH 7 are similar, compound I is in general more reactive towards organic substrates than compound II. The different reactivities have until now remained unexplained. In this study, the reactions of compounds I and II of peroxidase from horseradish with phenols were analyzed using the Marcus equation of electron-transfer. Both reactions exhibit similar reorganization energies, and the different reactivities of the two enzyme states can be ascribed to a higher apparent rate of activationless electron-transfer in the compound I reactions. This can be attributed to the shorter electron-tunneling distance on electron-transfer to the porphyrin radical cation in compound I, compared to electron-transfer to the iron ion in compound II.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>9256240</pmid><doi>10.1016/S0014-5793(97)00792-8</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1997-07, Vol.412 (2), p.305-308 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_79191838 |
| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Catalysis Electron-transfer Heme - chemistry Heme peroxidase Kinetics Marcus equation Peroxidases - chemistry Phenols - chemistry Phenoxyl radical Stopped-flow Substrate Specificity Thermodynamics |
| title | Interpretation of the reactivity of peroxidase compounds I and II with phenols by the Marcus equation |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-15T00%3A36%3A03IST&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=Interpretation%20of%20the%20reactivity%20of%20peroxidase%20compounds%20I%20and%20II%20with%20phenols%20by%20the%20Marcus%20equation&rft.jtitle=FEBS%20letters&rft.au=Folkes,%20Lisa%20K&rft.date=1997-07-28&rft.volume=412&rft.issue=2&rft.spage=305&rft.epage=308&rft.pages=305-308&rft.issn=0014-5793&rft.eissn=1873-3468&rft_id=info:doi/10.1016/S0014-5793(97)00792-8&rft_dat=%3Cproquest_cross%3E79191838%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=79191838&rft_id=info:pmid/9256240&rft_els_id=S0014579397007928&rfr_iscdi=true |