Reductive activation of potential antitumor bis(aziridinyl)benzoquinones by xanthine oxidase: Competition between oxygen reduction and quinone reduction
The reduction of a series of 2,5-bis(1-aziridinyl)-1,4-benzoquinone (BABQ) derivatives with various 3,6 substituents by the enzyme xanthine oxidase has been studied. The reduction rate has been assayed by measuring the rate of reduction of cytochrome c, which is very efficiently reduced by reduced B...
Gespeichert in:
| Veröffentlicht in: | Archives of biochemistry and biophysics 1990-02, Vol.277 (1), p.137-142 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 142 |
|---|---|
| container_issue | 1 |
| container_start_page | 137 |
| container_title | Archives of biochemistry and biophysics |
| container_volume | 277 |
| creator | Lusthof, K.J. Richter, W. de Mol, N.J. Janssen, L.H.M. Verboom, W. Reinhoudt, D.N. |
| description | The reduction of a series of 2,5-bis(1-aziridinyl)-1,4-benzoquinone (BABQ) derivatives with various 3,6 substituents by the enzyme xanthine oxidase has been studied. The reduction rate has been assayed by measuring the rate of reduction of cytochrome
c, which is very efficiently reduced by reduced BABQ species. Under nitrogen, the reduction rate correlated with the quinone reduction potential and steric parameters. Comparing reduction rates under nitrogen and air demonstrates that at BABQ concentrations > 25 μ
m the competition for electrons from xanthine oxidase between oxygen and the BABQ derivative is dominated by the latter. This is also confirmed by the effect of superoxide dismutase (SOD): in the presence of a BABQ derivative, cytochrome
c reduction can be totally inhibited by SOD, although the required amount of SOD depends on the redox potential of the quinones. This indicates that SOD causes the equilibrium between semiquinone and superoxide to shift, resulting in a decrease of the semiquinone concentration. It is concluded that reduction by xanthine oxidase is a simple and effective method for reducing aziridinylbenzoquinones. |
| doi_str_mv | 10.1016/0003-9861(90)90561-C |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_15602447</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>000398619090561C</els_id><sourcerecordid>15602447</sourcerecordid><originalsourceid>FETCH-LOGICAL-c464t-1174791347dafff8c1e18dde5b3bb79eb6cba57cfd0348e5b839c8cad12022f53</originalsourceid><addsrcrecordid>eNp9kcuKFTEQhoMo43H0DRSyUWYWrUl3-hIXgjTeYEAQXYdcKhrpTo5JejxnnsTHNe1pZnaufqj660ulfoSeUvKSEtq9IoQ0FR86esHJJSdtR6vxHtpRwruKNAO7j3a3lofoUUo_CaGUdfUZOqtpy3jb7tCfL2AWnd01YLmKzC54HCzehww-OzlhWSQvc4hYuXQhb1x0xvnjdKnA34Rfi_PBQ8LqiA_F-sN5wOHgjEzwGo9h3kMZX6EK8m-AAj8cvxeJp4dLQ3qDN8xd9TF6YOWU4Mmm5-jb-3dfx4_V1ecPn8a3V5VmHcsVpT3rOW1Yb6S1dtAU6GAMtKpRquegOq1k22trSMOGUh4argctDa1JXdu2OUcvTtx9LH-BlMXskoZpkh7CkgRtO1Iz1hcjOxl1DClFsGIf3SzjUVAi1kDEem2xXltwIv4FIsYy9mzjL2oGczu0JVD6z7e-TFpONkqvXbpj844UUlN8b04-KMe4dhBF0g68BuMi6CxMcP9f5C_Jn6zJ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15602447</pqid></control><display><type>article</type><title>Reductive activation of potential antitumor bis(aziridinyl)benzoquinones by xanthine oxidase: Competition between oxygen reduction and quinone reduction</title><source>MEDLINE</source><source>Access via ScienceDirect (Elsevier)</source><creator>Lusthof, K.J. ; Richter, W. ; de Mol, N.J. ; Janssen, L.H.M. ; Verboom, W. ; Reinhoudt, D.N.</creator><creatorcontrib>Lusthof, K.J. ; Richter, W. ; de Mol, N.J. ; Janssen, L.H.M. ; Verboom, W. ; Reinhoudt, D.N.</creatorcontrib><description>The reduction of a series of 2,5-bis(1-aziridinyl)-1,4-benzoquinone (BABQ) derivatives with various 3,6 substituents by the enzyme xanthine oxidase has been studied. The reduction rate has been assayed by measuring the rate of reduction of cytochrome
c, which is very efficiently reduced by reduced BABQ species. Under nitrogen, the reduction rate correlated with the quinone reduction potential and steric parameters. Comparing reduction rates under nitrogen and air demonstrates that at BABQ concentrations > 25 μ
m the competition for electrons from xanthine oxidase between oxygen and the BABQ derivative is dominated by the latter. This is also confirmed by the effect of superoxide dismutase (SOD): in the presence of a BABQ derivative, cytochrome
c reduction can be totally inhibited by SOD, although the required amount of SOD depends on the redox potential of the quinones. This indicates that SOD causes the equilibrium between semiquinone and superoxide to shift, resulting in a decrease of the semiquinone concentration. It is concluded that reduction by xanthine oxidase is a simple and effective method for reducing aziridinylbenzoquinones.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(90)90561-C</identifier><identifier>PMID: 2154955</identifier><identifier>CODEN: ABBIA4</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Antineoplastic agents ; Antineoplastic Agents - metabolism ; Aziridines - metabolism ; benzoquinone ; Benzoquinones ; Biological and medical sciences ; Biotransformation ; Catalase - metabolism ; Cyclohexenes ; Cytochrome c Group - metabolism ; General aspects ; Kinetics ; Medical sciences ; Oxidation-Reduction ; Pharmacology. Drug treatments ; Structure-Activity Relationship ; Superoxide Dismutase - metabolism ; Xanthine Oxidase - metabolism</subject><ispartof>Archives of biochemistry and biophysics, 1990-02, Vol.277 (1), p.137-142</ispartof><rights>1990</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c464t-1174791347dafff8c1e18dde5b3bb79eb6cba57cfd0348e5b839c8cad12022f53</citedby><cites>FETCH-LOGICAL-c464t-1174791347dafff8c1e18dde5b3bb79eb6cba57cfd0348e5b839c8cad12022f53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0003-9861(90)90561-C$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19600563$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2154955$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lusthof, K.J.</creatorcontrib><creatorcontrib>Richter, W.</creatorcontrib><creatorcontrib>de Mol, N.J.</creatorcontrib><creatorcontrib>Janssen, L.H.M.</creatorcontrib><creatorcontrib>Verboom, W.</creatorcontrib><creatorcontrib>Reinhoudt, D.N.</creatorcontrib><title>Reductive activation of potential antitumor bis(aziridinyl)benzoquinones by xanthine oxidase: Competition between oxygen reduction and quinone reduction</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>The reduction of a series of 2,5-bis(1-aziridinyl)-1,4-benzoquinone (BABQ) derivatives with various 3,6 substituents by the enzyme xanthine oxidase has been studied. The reduction rate has been assayed by measuring the rate of reduction of cytochrome
c, which is very efficiently reduced by reduced BABQ species. Under nitrogen, the reduction rate correlated with the quinone reduction potential and steric parameters. Comparing reduction rates under nitrogen and air demonstrates that at BABQ concentrations > 25 μ
m the competition for electrons from xanthine oxidase between oxygen and the BABQ derivative is dominated by the latter. This is also confirmed by the effect of superoxide dismutase (SOD): in the presence of a BABQ derivative, cytochrome
c reduction can be totally inhibited by SOD, although the required amount of SOD depends on the redox potential of the quinones. This indicates that SOD causes the equilibrium between semiquinone and superoxide to shift, resulting in a decrease of the semiquinone concentration. It is concluded that reduction by xanthine oxidase is a simple and effective method for reducing aziridinylbenzoquinones.</description><subject>Antineoplastic agents</subject><subject>Antineoplastic Agents - metabolism</subject><subject>Aziridines - metabolism</subject><subject>benzoquinone</subject><subject>Benzoquinones</subject><subject>Biological and medical sciences</subject><subject>Biotransformation</subject><subject>Catalase - metabolism</subject><subject>Cyclohexenes</subject><subject>Cytochrome c Group - metabolism</subject><subject>General aspects</subject><subject>Kinetics</subject><subject>Medical sciences</subject><subject>Oxidation-Reduction</subject><subject>Pharmacology. Drug treatments</subject><subject>Structure-Activity Relationship</subject><subject>Superoxide Dismutase - metabolism</subject><subject>Xanthine Oxidase - metabolism</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kcuKFTEQhoMo43H0DRSyUWYWrUl3-hIXgjTeYEAQXYdcKhrpTo5JejxnnsTHNe1pZnaufqj660ulfoSeUvKSEtq9IoQ0FR86esHJJSdtR6vxHtpRwruKNAO7j3a3lofoUUo_CaGUdfUZOqtpy3jb7tCfL2AWnd01YLmKzC54HCzehww-OzlhWSQvc4hYuXQhb1x0xvnjdKnA34Rfi_PBQ8LqiA_F-sN5wOHgjEzwGo9h3kMZX6EK8m-AAj8cvxeJp4dLQ3qDN8xd9TF6YOWU4Mmm5-jb-3dfx4_V1ecPn8a3V5VmHcsVpT3rOW1Yb6S1dtAU6GAMtKpRquegOq1k22trSMOGUh4argctDa1JXdu2OUcvTtx9LH-BlMXskoZpkh7CkgRtO1Iz1hcjOxl1DClFsGIf3SzjUVAi1kDEem2xXltwIv4FIsYy9mzjL2oGczu0JVD6z7e-TFpONkqvXbpj844UUlN8b04-KMe4dhBF0g68BuMi6CxMcP9f5C_Jn6zJ</recordid><startdate>19900215</startdate><enddate>19900215</enddate><creator>Lusthof, K.J.</creator><creator>Richter, W.</creator><creator>de Mol, N.J.</creator><creator>Janssen, L.H.M.</creator><creator>Verboom, W.</creator><creator>Reinhoudt, D.N.</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope></search><sort><creationdate>19900215</creationdate><title>Reductive activation of potential antitumor bis(aziridinyl)benzoquinones by xanthine oxidase: Competition between oxygen reduction and quinone reduction</title><author>Lusthof, K.J. ; Richter, W. ; de Mol, N.J. ; Janssen, L.H.M. ; Verboom, W. ; Reinhoudt, D.N.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c464t-1174791347dafff8c1e18dde5b3bb79eb6cba57cfd0348e5b839c8cad12022f53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Antineoplastic agents</topic><topic>Antineoplastic Agents - metabolism</topic><topic>Aziridines - metabolism</topic><topic>benzoquinone</topic><topic>Benzoquinones</topic><topic>Biological and medical sciences</topic><topic>Biotransformation</topic><topic>Catalase - metabolism</topic><topic>Cyclohexenes</topic><topic>Cytochrome c Group - metabolism</topic><topic>General aspects</topic><topic>Kinetics</topic><topic>Medical sciences</topic><topic>Oxidation-Reduction</topic><topic>Pharmacology. Drug treatments</topic><topic>Structure-Activity Relationship</topic><topic>Superoxide Dismutase - metabolism</topic><topic>Xanthine Oxidase - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lusthof, K.J.</creatorcontrib><creatorcontrib>Richter, W.</creatorcontrib><creatorcontrib>de Mol, N.J.</creatorcontrib><creatorcontrib>Janssen, L.H.M.</creatorcontrib><creatorcontrib>Verboom, W.</creatorcontrib><creatorcontrib>Reinhoudt, D.N.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lusthof, K.J.</au><au>Richter, W.</au><au>de Mol, N.J.</au><au>Janssen, L.H.M.</au><au>Verboom, W.</au><au>Reinhoudt, D.N.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Reductive activation of potential antitumor bis(aziridinyl)benzoquinones by xanthine oxidase: Competition between oxygen reduction and quinone reduction</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1990-02-15</date><risdate>1990</risdate><volume>277</volume><issue>1</issue><spage>137</spage><epage>142</epage><pages>137-142</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><coden>ABBIA4</coden><abstract>The reduction of a series of 2,5-bis(1-aziridinyl)-1,4-benzoquinone (BABQ) derivatives with various 3,6 substituents by the enzyme xanthine oxidase has been studied. The reduction rate has been assayed by measuring the rate of reduction of cytochrome
c, which is very efficiently reduced by reduced BABQ species. Under nitrogen, the reduction rate correlated with the quinone reduction potential and steric parameters. Comparing reduction rates under nitrogen and air demonstrates that at BABQ concentrations > 25 μ
m the competition for electrons from xanthine oxidase between oxygen and the BABQ derivative is dominated by the latter. This is also confirmed by the effect of superoxide dismutase (SOD): in the presence of a BABQ derivative, cytochrome
c reduction can be totally inhibited by SOD, although the required amount of SOD depends on the redox potential of the quinones. This indicates that SOD causes the equilibrium between semiquinone and superoxide to shift, resulting in a decrease of the semiquinone concentration. It is concluded that reduction by xanthine oxidase is a simple and effective method for reducing aziridinylbenzoquinones.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>2154955</pmid><doi>10.1016/0003-9861(90)90561-C</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-9861 |
| ispartof | Archives of biochemistry and biophysics, 1990-02, Vol.277 (1), p.137-142 |
| issn | 0003-9861 1096-0384 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_15602447 |
| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Antineoplastic agents Antineoplastic Agents - metabolism Aziridines - metabolism benzoquinone Benzoquinones Biological and medical sciences Biotransformation Catalase - metabolism Cyclohexenes Cytochrome c Group - metabolism General aspects Kinetics Medical sciences Oxidation-Reduction Pharmacology. Drug treatments Structure-Activity Relationship Superoxide Dismutase - metabolism Xanthine Oxidase - metabolism |
| title | Reductive activation of potential antitumor bis(aziridinyl)benzoquinones by xanthine oxidase: Competition between oxygen reduction and quinone reduction |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-02T17%3A35%3A50IST&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=Reductive%20activation%20of%20potential%20antitumor%20bis(aziridinyl)benzoquinones%20by%20xanthine%20oxidase:%20Competition%20between%20oxygen%20reduction%20and%20quinone%20reduction&rft.jtitle=Archives%20of%20biochemistry%20and%20biophysics&rft.au=Lusthof,%20K.J.&rft.date=1990-02-15&rft.volume=277&rft.issue=1&rft.spage=137&rft.epage=142&rft.pages=137-142&rft.issn=0003-9861&rft.eissn=1096-0384&rft.coden=ABBIA4&rft_id=info:doi/10.1016/0003-9861(90)90561-C&rft_dat=%3Cproquest_cross%3E15602447%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=15602447&rft_id=info:pmid/2154955&rft_els_id=000398619090561C&rfr_iscdi=true |