Human Cytochrome P450 2C9 and Its Polymorphic Modifications: Electroanalysis, Catalytic Properties, and Approaches to the Regulation of Enzymatic Activity

The electrochemical properties of cytochrome P450 2C9 (CYP2C9) and polymorphic modifications P450 2C9*2 (CYP2C9*2) and P450 2C9*3 (CYP2C9*3) were studied. To analyze the comparative electrochemical and electrocatalytic activity, the enzymes were immobilized on electrodes modified with a membrane-lik...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Processes 2022-02, Vol.10 (2), p.383
Hauptverfasser: Shumyantseva, Victoria V., Bulko, Tatiana V., Koroleva, Polina I., Shikh, Evgeniya V., Makhova, Anna A., Kisel, Maryia S., Haidukevich, Irina V., Gilep, Andrei A.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page
container_issue 2
container_start_page 383
container_title Processes
container_volume 10
creator Shumyantseva, Victoria V.
Bulko, Tatiana V.
Koroleva, Polina I.
Shikh, Evgeniya V.
Makhova, Anna A.
Kisel, Maryia S.
Haidukevich, Irina V.
Gilep, Andrei A.
description The electrochemical properties of cytochrome P450 2C9 (CYP2C9) and polymorphic modifications P450 2C9*2 (CYP2C9*2) and P450 2C9*3 (CYP2C9*3) were studied. To analyze the comparative electrochemical and electrocatalytic activity, the enzymes were immobilized on electrodes modified with a membrane-like synthetic surfactant (didodecyldimethylammonium bromide (DDAB)). An adequate choice of the type of modified electrode was confirmed by cyclic voltammetry of cytochromes P450 under anaerobic conditions, demonstrating well-defined peaks of reduction and oxidation of the heme iron. The midpoint potential, Emid, of cytochrome P450 2C9 is −0.318 ± 0.01 V, and Emid = −0.324 ± 0.01 V, and Emid = −0.318 ± 0.03 V for allelic variant 2C9*2 and allelic variant 2C9*3, respectively. In the presence of substrate diclofenac under aerobic conditions, cytochrome P450 2C9 and its polymorphic modifications P450 2C9*2 and P450 2C9*3 exhibit catalytic properties. Stimulation of the metabolism of diclofenac by cytochrome P450 2C9 in the presence of antioxidant medications mexidol and taurine was shown.
doi_str_mv 10.3390/pr10020383
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_journals_2633049333</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2633049333</sourcerecordid><originalsourceid>FETCH-LOGICAL-c295t-44d0293e56064d94e935715a5081e507373ff3a80993d6efa3676030277400ab3</originalsourceid><addsrcrecordid>eNpNUNFKw0AQPETBUvviFxz4JlY3t0ku51sJ1RYqFtHncCYXcyXJxbuLED_FrzW1gs7LDsvsMDuEnAdwjSjgprMBAANM8IhMGGN8LnjAj__xUzJzbgcjRIBJFE_I16pvZEvTwZu8sqZRdBtGQFkqqGwLuvaObk09NMZ2lc7pgyl0qXPptWndLV3WKvfWyFbWg9PuiqbSj9SPyq01nbJeq3G7d1p03SjMK-WoN9RXij6pt77-caKmpMv2c2jk_nKRe_2h_XBGTkpZOzX7nVPycrd8TlfzzeP9Ol1s5jkTkZ-HYQFMoIpiiMNChEpgxINIRpAEKgKOHMsSZQJCYBGrUmLMY0BgnIcA8hWn5OLgOwZ875Xz2c70dnzJZSxGhFDgiCm5PKhya5yzqsw6qxtphyyAbF9_9lc_fgO_Jncd</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2633049333</pqid></control><display><type>article</type><title>Human Cytochrome P450 2C9 and Its Polymorphic Modifications: Electroanalysis, Catalytic Properties, and Approaches to the Regulation of Enzymatic Activity</title><source>MDPI - Multidisciplinary Digital Publishing Institute</source><source>EZB-FREE-00999 freely available EZB journals</source><creator>Shumyantseva, Victoria V. ; Bulko, Tatiana V. ; Koroleva, Polina I. ; Shikh, Evgeniya V. ; Makhova, Anna A. ; Kisel, Maryia S. ; Haidukevich, Irina V. ; Gilep, Andrei A.</creator><creatorcontrib>Shumyantseva, Victoria V. ; Bulko, Tatiana V. ; Koroleva, Polina I. ; Shikh, Evgeniya V. ; Makhova, Anna A. ; Kisel, Maryia S. ; Haidukevich, Irina V. ; Gilep, Andrei A.</creatorcontrib><description>The electrochemical properties of cytochrome P450 2C9 (CYP2C9) and polymorphic modifications P450 2C9*2 (CYP2C9*2) and P450 2C9*3 (CYP2C9*3) were studied. To analyze the comparative electrochemical and electrocatalytic activity, the enzymes were immobilized on electrodes modified with a membrane-like synthetic surfactant (didodecyldimethylammonium bromide (DDAB)). An adequate choice of the type of modified electrode was confirmed by cyclic voltammetry of cytochromes P450 under anaerobic conditions, demonstrating well-defined peaks of reduction and oxidation of the heme iron. The midpoint potential, Emid, of cytochrome P450 2C9 is −0.318 ± 0.01 V, and Emid = −0.324 ± 0.01 V, and Emid = −0.318 ± 0.03 V for allelic variant 2C9*2 and allelic variant 2C9*3, respectively. In the presence of substrate diclofenac under aerobic conditions, cytochrome P450 2C9 and its polymorphic modifications P450 2C9*2 and P450 2C9*3 exhibit catalytic properties. Stimulation of the metabolism of diclofenac by cytochrome P450 2C9 in the presence of antioxidant medications mexidol and taurine was shown.</description><identifier>ISSN: 2227-9717</identifier><identifier>EISSN: 2227-9717</identifier><identifier>DOI: 10.3390/pr10020383</identifier><language>eng</language><publisher>Basel: MDPI AG</publisher><subject>Aerobic conditions ; Anaerobic conditions ; Antioxidants ; Catalysis ; Cytochrome ; Cytochrome P450 ; Cytochromes P450 ; Diclofenac ; Drug interactions ; Electrochemical analysis ; Electrodes ; Electrolytic analysis ; Enzymatic activity ; Enzymes ; Experiments ; Heme ; Metabolism ; Mutation ; Nonsteroidal anti-inflammatory drugs ; Oxidation ; Pharmacokinetics ; Proteins ; Software ; Substrates ; Taurine</subject><ispartof>Processes, 2022-02, Vol.10 (2), p.383</ispartof><rights>2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c295t-44d0293e56064d94e935715a5081e507373ff3a80993d6efa3676030277400ab3</citedby><cites>FETCH-LOGICAL-c295t-44d0293e56064d94e935715a5081e507373ff3a80993d6efa3676030277400ab3</cites><orcidid>0000-0003-2802-5747 ; 0000-0003-3432-0064</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids></links><search><creatorcontrib>Shumyantseva, Victoria V.</creatorcontrib><creatorcontrib>Bulko, Tatiana V.</creatorcontrib><creatorcontrib>Koroleva, Polina I.</creatorcontrib><creatorcontrib>Shikh, Evgeniya V.</creatorcontrib><creatorcontrib>Makhova, Anna A.</creatorcontrib><creatorcontrib>Kisel, Maryia S.</creatorcontrib><creatorcontrib>Haidukevich, Irina V.</creatorcontrib><creatorcontrib>Gilep, Andrei A.</creatorcontrib><title>Human Cytochrome P450 2C9 and Its Polymorphic Modifications: Electroanalysis, Catalytic Properties, and Approaches to the Regulation of Enzymatic Activity</title><title>Processes</title><description>The electrochemical properties of cytochrome P450 2C9 (CYP2C9) and polymorphic modifications P450 2C9*2 (CYP2C9*2) and P450 2C9*3 (CYP2C9*3) were studied. To analyze the comparative electrochemical and electrocatalytic activity, the enzymes were immobilized on electrodes modified with a membrane-like synthetic surfactant (didodecyldimethylammonium bromide (DDAB)). An adequate choice of the type of modified electrode was confirmed by cyclic voltammetry of cytochromes P450 under anaerobic conditions, demonstrating well-defined peaks of reduction and oxidation of the heme iron. The midpoint potential, Emid, of cytochrome P450 2C9 is −0.318 ± 0.01 V, and Emid = −0.324 ± 0.01 V, and Emid = −0.318 ± 0.03 V for allelic variant 2C9*2 and allelic variant 2C9*3, respectively. In the presence of substrate diclofenac under aerobic conditions, cytochrome P450 2C9 and its polymorphic modifications P450 2C9*2 and P450 2C9*3 exhibit catalytic properties. Stimulation of the metabolism of diclofenac by cytochrome P450 2C9 in the presence of antioxidant medications mexidol and taurine was shown.</description><subject>Aerobic conditions</subject><subject>Anaerobic conditions</subject><subject>Antioxidants</subject><subject>Catalysis</subject><subject>Cytochrome</subject><subject>Cytochrome P450</subject><subject>Cytochromes P450</subject><subject>Diclofenac</subject><subject>Drug interactions</subject><subject>Electrochemical analysis</subject><subject>Electrodes</subject><subject>Electrolytic analysis</subject><subject>Enzymatic activity</subject><subject>Enzymes</subject><subject>Experiments</subject><subject>Heme</subject><subject>Metabolism</subject><subject>Mutation</subject><subject>Nonsteroidal anti-inflammatory drugs</subject><subject>Oxidation</subject><subject>Pharmacokinetics</subject><subject>Proteins</subject><subject>Software</subject><subject>Substrates</subject><subject>Taurine</subject><issn>2227-9717</issn><issn>2227-9717</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNpNUNFKw0AQPETBUvviFxz4JlY3t0ku51sJ1RYqFtHncCYXcyXJxbuLED_FrzW1gs7LDsvsMDuEnAdwjSjgprMBAANM8IhMGGN8LnjAj__xUzJzbgcjRIBJFE_I16pvZEvTwZu8sqZRdBtGQFkqqGwLuvaObk09NMZ2lc7pgyl0qXPptWndLV3WKvfWyFbWg9PuiqbSj9SPyq01nbJeq3G7d1p03SjMK-WoN9RXij6pt77-caKmpMv2c2jk_nKRe_2h_XBGTkpZOzX7nVPycrd8TlfzzeP9Ol1s5jkTkZ-HYQFMoIpiiMNChEpgxINIRpAEKgKOHMsSZQJCYBGrUmLMY0BgnIcA8hWn5OLgOwZ875Xz2c70dnzJZSxGhFDgiCm5PKhya5yzqsw6qxtphyyAbF9_9lc_fgO_Jncd</recordid><startdate>20220201</startdate><enddate>20220201</enddate><creator>Shumyantseva, Victoria V.</creator><creator>Bulko, Tatiana V.</creator><creator>Koroleva, Polina I.</creator><creator>Shikh, Evgeniya V.</creator><creator>Makhova, Anna A.</creator><creator>Kisel, Maryia S.</creator><creator>Haidukevich, Irina V.</creator><creator>Gilep, Andrei A.</creator><general>MDPI AG</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7SR</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>COVID</scope><scope>D1I</scope><scope>DWQXO</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>JG9</scope><scope>KB.</scope><scope>LK8</scope><scope>M7P</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><orcidid>https://orcid.org/0000-0003-2802-5747</orcidid><orcidid>https://orcid.org/0000-0003-3432-0064</orcidid></search><sort><creationdate>20220201</creationdate><title>Human Cytochrome P450 2C9 and Its Polymorphic Modifications: Electroanalysis, Catalytic Properties, and Approaches to the Regulation of Enzymatic Activity</title><author>Shumyantseva, Victoria V. ; Bulko, Tatiana V. ; Koroleva, Polina I. ; Shikh, Evgeniya V. ; Makhova, Anna A. ; Kisel, Maryia S. ; Haidukevich, Irina V. ; Gilep, Andrei A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c295t-44d0293e56064d94e935715a5081e507373ff3a80993d6efa3676030277400ab3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Aerobic conditions</topic><topic>Anaerobic conditions</topic><topic>Antioxidants</topic><topic>Catalysis</topic><topic>Cytochrome</topic><topic>Cytochrome P450</topic><topic>Cytochromes P450</topic><topic>Diclofenac</topic><topic>Drug interactions</topic><topic>Electrochemical analysis</topic><topic>Electrodes</topic><topic>Electrolytic analysis</topic><topic>Enzymatic activity</topic><topic>Enzymes</topic><topic>Experiments</topic><topic>Heme</topic><topic>Metabolism</topic><topic>Mutation</topic><topic>Nonsteroidal anti-inflammatory drugs</topic><topic>Oxidation</topic><topic>Pharmacokinetics</topic><topic>Proteins</topic><topic>Software</topic><topic>Substrates</topic><topic>Taurine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shumyantseva, Victoria V.</creatorcontrib><creatorcontrib>Bulko, Tatiana V.</creatorcontrib><creatorcontrib>Koroleva, Polina I.</creatorcontrib><creatorcontrib>Shikh, Evgeniya V.</creatorcontrib><creatorcontrib>Makhova, Anna A.</creatorcontrib><creatorcontrib>Kisel, Maryia S.</creatorcontrib><creatorcontrib>Haidukevich, Irina V.</creatorcontrib><creatorcontrib>Gilep, Andrei A.</creatorcontrib><collection>CrossRef</collection><collection>Engineered Materials Abstracts</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Materials Science &amp; Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>Coronavirus Research Database</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>Materials Research Database</collection><collection>Materials Science Database</collection><collection>ProQuest Biological Science Collection</collection><collection>Biological Science Database</collection><collection>Materials Science Collection</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><jtitle>Processes</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shumyantseva, Victoria V.</au><au>Bulko, Tatiana V.</au><au>Koroleva, Polina I.</au><au>Shikh, Evgeniya V.</au><au>Makhova, Anna A.</au><au>Kisel, Maryia S.</au><au>Haidukevich, Irina V.</au><au>Gilep, Andrei A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Human Cytochrome P450 2C9 and Its Polymorphic Modifications: Electroanalysis, Catalytic Properties, and Approaches to the Regulation of Enzymatic Activity</atitle><jtitle>Processes</jtitle><date>2022-02-01</date><risdate>2022</risdate><volume>10</volume><issue>2</issue><spage>383</spage><pages>383-</pages><issn>2227-9717</issn><eissn>2227-9717</eissn><abstract>The electrochemical properties of cytochrome P450 2C9 (CYP2C9) and polymorphic modifications P450 2C9*2 (CYP2C9*2) and P450 2C9*3 (CYP2C9*3) were studied. To analyze the comparative electrochemical and electrocatalytic activity, the enzymes were immobilized on electrodes modified with a membrane-like synthetic surfactant (didodecyldimethylammonium bromide (DDAB)). An adequate choice of the type of modified electrode was confirmed by cyclic voltammetry of cytochromes P450 under anaerobic conditions, demonstrating well-defined peaks of reduction and oxidation of the heme iron. The midpoint potential, Emid, of cytochrome P450 2C9 is −0.318 ± 0.01 V, and Emid = −0.324 ± 0.01 V, and Emid = −0.318 ± 0.03 V for allelic variant 2C9*2 and allelic variant 2C9*3, respectively. In the presence of substrate diclofenac under aerobic conditions, cytochrome P450 2C9 and its polymorphic modifications P450 2C9*2 and P450 2C9*3 exhibit catalytic properties. Stimulation of the metabolism of diclofenac by cytochrome P450 2C9 in the presence of antioxidant medications mexidol and taurine was shown.</abstract><cop>Basel</cop><pub>MDPI AG</pub><doi>10.3390/pr10020383</doi><orcidid>https://orcid.org/0000-0003-2802-5747</orcidid><orcidid>https://orcid.org/0000-0003-3432-0064</orcidid><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 2227-9717
ispartof Processes, 2022-02, Vol.10 (2), p.383
issn 2227-9717
2227-9717
language eng
recordid cdi_proquest_journals_2633049333
source MDPI - Multidisciplinary Digital Publishing Institute; EZB-FREE-00999 freely available EZB journals
subjects Aerobic conditions
Anaerobic conditions
Antioxidants
Catalysis
Cytochrome
Cytochrome P450
Cytochromes P450
Diclofenac
Drug interactions
Electrochemical analysis
Electrodes
Electrolytic analysis
Enzymatic activity
Enzymes
Experiments
Heme
Metabolism
Mutation
Nonsteroidal anti-inflammatory drugs
Oxidation
Pharmacokinetics
Proteins
Software
Substrates
Taurine
title Human Cytochrome P450 2C9 and Its Polymorphic Modifications: Electroanalysis, Catalytic Properties, and Approaches to the Regulation of Enzymatic Activity
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-10T14%3A18%3A39IST&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=Human%20Cytochrome%20P450%202C9%20and%20Its%20Polymorphic%20Modifications:%20Electroanalysis,%20Catalytic%20Properties,%20and%20Approaches%20to%20the%20Regulation%20of%20Enzymatic%20Activity&rft.jtitle=Processes&rft.au=Shumyantseva,%20Victoria%20V.&rft.date=2022-02-01&rft.volume=10&rft.issue=2&rft.spage=383&rft.pages=383-&rft.issn=2227-9717&rft.eissn=2227-9717&rft_id=info:doi/10.3390/pr10020383&rft_dat=%3Cproquest_cross%3E2633049333%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=2633049333&rft_id=info:pmid/&rfr_iscdi=true