On the mechanism of rotenone-insensitive reduction of quinones by mitochondrial NADH:ubiquinone reductase The high affinity binding of NAD + and NADH to the reduced enzyme form
NADH acts as an incomplete competitive inhibitor for 5,8-dioxy-1,4-naphtoquinone during its rotenone-insensitive reduction by mitochondrial NADH:ubiquinone reductase. NAD + and ADP-ribose act as incomplete mixed-type inhibitors. K i of NAD + and NADH towards quinone are about one order less than tow...
Gespeichert in:
| Veröffentlicht in: | FEBS letters 1991-06, Vol.284 (2), p.192-194 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 194 |
|---|---|
| container_issue | 2 |
| container_start_page | 192 |
| container_title | FEBS letters |
| container_volume | 284 |
| creator | Čénas, Narimantas K. Bironaité, Daiva A. Kulys, Juozas J. |
| description | NADH acts as an incomplete competitive inhibitor for 5,8-dioxy-1,4-naphtoquinone during its rotenone-insensitive reduction by mitochondrial NADH:ubiquinone reductase. NAD
+ and ADP-ribose act as incomplete mixed-type inhibitors.
K
i of NAD
+ and NADH towards quinone are about one order less than towards ferricyanide. The bimolecular rate constant of the reduction of the enzyme by NADH in the quinone reductase reaction is about 2 times less than that of ferricyanide reductase reaction. These data indicate that the reduction site of 5,8-dioxy-1,4-naphtoquinone is close to NAD
+/NADH and ferricyanide binding site. It seems that during the steady-state reduction of ferricyanide and 5,8-dioxy-1,4-naphtoquinone these oxidizers react with NADH:ubiquinone reductase reduced to different extents. |
| doi_str_mv | 10.1016/0014-5793(91)80682-S |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_80656534</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>001457939180682S</els_id><sourcerecordid>80656534</sourcerecordid><originalsourceid>FETCH-LOGICAL-c420S-e233c0ff9c8888ee1d687d80e39171a1fb2def494ff92a66e4ac6e120478aacb3</originalsourceid><addsrcrecordid>eNqNkc1u1TAQhS0EKpfCG4DkFaJCATvxzQ8LpLb0UqSKLm5ZW449aQYldmsnReGpeESc5Ap2CG8sz3znjDWHkJecveOM5-8Z4yLZFlX2puInJcvLNNk_IhteFlmSibx8TDZ_kKfkWQjfWXyXvDoiR7xi21xUG_Lr2tKhBdqDbpXF0FPXUO8GsM5CgjaADTjgA1APZtQDOjsT9yPOQKD1RHscnG6dNR5VR7-efrr8MNZ4IA4yFYDexDEt3rZUNQ1aHCZaozVob2fDKKNvqbJmMaCDW361iMFQsD-nHmjjfP-cPGlUF-DF4T4m33YXN-eXydX15y_np1eJFinbJ5BmmWZNU-kyHgBu8rIwJYOs4gVXvKlTA42oRERSlecglM6Bp0wUpVK6zo7J69X3zrv7EcIgewwauk5ZcGOQceHbfJuJCIoV1N6F4KGRdx575SfJmZyDknMKck5BVlwuQcl9lL06-I91D-avaE0m9ndr_wd2MP2Xp9xdnKVzY65XfKnOgz6uRhC39YDgZdAINq4VPehBGof__ulvqWy48w</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>80656534</pqid></control><display><type>article</type><title>On the mechanism of rotenone-insensitive reduction of quinones by mitochondrial NADH:ubiquinone reductase The high affinity binding of NAD + and NADH to the reduced enzyme form</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>Čénas, Narimantas K. ; Bironaité, Daiva A. ; Kulys, Juozas J.</creator><creatorcontrib>Čénas, Narimantas K. ; Bironaité, Daiva A. ; Kulys, Juozas J.</creatorcontrib><description>NADH acts as an incomplete competitive inhibitor for 5,8-dioxy-1,4-naphtoquinone during its rotenone-insensitive reduction by mitochondrial NADH:ubiquinone reductase. NAD
+ and ADP-ribose act as incomplete mixed-type inhibitors.
K
i of NAD
+ and NADH towards quinone are about one order less than towards ferricyanide. The bimolecular rate constant of the reduction of the enzyme by NADH in the quinone reductase reaction is about 2 times less than that of ferricyanide reductase reaction. These data indicate that the reduction site of 5,8-dioxy-1,4-naphtoquinone is close to NAD
+/NADH and ferricyanide binding site. It seems that during the steady-state reduction of ferricyanide and 5,8-dioxy-1,4-naphtoquinone these oxidizers react with NADH:ubiquinone reductase reduced to different extents.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(91)80682-S</identifier><identifier>PMID: 1905649</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Animals ; Binding, Competitive ; biomolecular rate constant ; Cattle ; Electron acceptor ; Mitochondria, Heart - enzymology ; NAD - metabolism ; NAD(P)H Dehydrogenase (Quinone) ; NADH:ubiquinone reductase ; Naphthoquinones - metabolism ; Oxidation-Reduction ; Quinone Reductases - metabolism ; Rotenone - pharmacology ; Steady-state kinetics ; TN/K m ; turnover number</subject><ispartof>FEBS letters, 1991-06, Vol.284 (2), p.192-194</ispartof><rights>1991</rights><rights>FEBS Letters 284 (1991) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c420S-e233c0ff9c8888ee1d687d80e39171a1fb2def494ff92a66e4ac6e120478aacb3</citedby><cites>FETCH-LOGICAL-c420S-e233c0ff9c8888ee1d687d80e39171a1fb2def494ff92a66e4ac6e120478aacb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/001457939180682S$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1905649$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Čénas, Narimantas K.</creatorcontrib><creatorcontrib>Bironaité, Daiva A.</creatorcontrib><creatorcontrib>Kulys, Juozas J.</creatorcontrib><title>On the mechanism of rotenone-insensitive reduction of quinones by mitochondrial NADH:ubiquinone reductase The high affinity binding of NAD + and NADH to the reduced enzyme form</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>NADH acts as an incomplete competitive inhibitor for 5,8-dioxy-1,4-naphtoquinone during its rotenone-insensitive reduction by mitochondrial NADH:ubiquinone reductase. NAD
+ and ADP-ribose act as incomplete mixed-type inhibitors.
K
i of NAD
+ and NADH towards quinone are about one order less than towards ferricyanide. The bimolecular rate constant of the reduction of the enzyme by NADH in the quinone reductase reaction is about 2 times less than that of ferricyanide reductase reaction. These data indicate that the reduction site of 5,8-dioxy-1,4-naphtoquinone is close to NAD
+/NADH and ferricyanide binding site. It seems that during the steady-state reduction of ferricyanide and 5,8-dioxy-1,4-naphtoquinone these oxidizers react with NADH:ubiquinone reductase reduced to different extents.</description><subject>Animals</subject><subject>Binding, Competitive</subject><subject>biomolecular rate constant</subject><subject>Cattle</subject><subject>Electron acceptor</subject><subject>Mitochondria, Heart - enzymology</subject><subject>NAD - metabolism</subject><subject>NAD(P)H Dehydrogenase (Quinone)</subject><subject>NADH:ubiquinone reductase</subject><subject>Naphthoquinones - metabolism</subject><subject>Oxidation-Reduction</subject><subject>Quinone Reductases - metabolism</subject><subject>Rotenone - pharmacology</subject><subject>Steady-state kinetics</subject><subject>TN/K m</subject><subject>turnover number</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc1u1TAQhS0EKpfCG4DkFaJCATvxzQ8LpLb0UqSKLm5ZW449aQYldmsnReGpeESc5Ap2CG8sz3znjDWHkJecveOM5-8Z4yLZFlX2puInJcvLNNk_IhteFlmSibx8TDZ_kKfkWQjfWXyXvDoiR7xi21xUG_Lr2tKhBdqDbpXF0FPXUO8GsM5CgjaADTjgA1APZtQDOjsT9yPOQKD1RHscnG6dNR5VR7-efrr8MNZ4IA4yFYDexDEt3rZUNQ1aHCZaozVob2fDKKNvqbJmMaCDW361iMFQsD-nHmjjfP-cPGlUF-DF4T4m33YXN-eXydX15y_np1eJFinbJ5BmmWZNU-kyHgBu8rIwJYOs4gVXvKlTA42oRERSlecglM6Bp0wUpVK6zo7J69X3zrv7EcIgewwauk5ZcGOQceHbfJuJCIoV1N6F4KGRdx575SfJmZyDknMKck5BVlwuQcl9lL06-I91D-avaE0m9ndr_wd2MP2Xp9xdnKVzY65XfKnOgz6uRhC39YDgZdAINq4VPehBGof__ulvqWy48w</recordid><startdate>19910624</startdate><enddate>19910624</enddate><creator>Čénas, Narimantas K.</creator><creator>Bironaité, Daiva A.</creator><creator>Kulys, Juozas J.</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>19910624</creationdate><title>On the mechanism of rotenone-insensitive reduction of quinones by mitochondrial NADH:ubiquinone reductase The high affinity binding of NAD + and NADH to the reduced enzyme form</title><author>Čénas, Narimantas K. ; Bironaité, Daiva A. ; Kulys, Juozas J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c420S-e233c0ff9c8888ee1d687d80e39171a1fb2def494ff92a66e4ac6e120478aacb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Animals</topic><topic>Binding, Competitive</topic><topic>biomolecular rate constant</topic><topic>Cattle</topic><topic>Electron acceptor</topic><topic>Mitochondria, Heart - enzymology</topic><topic>NAD - metabolism</topic><topic>NAD(P)H Dehydrogenase (Quinone)</topic><topic>NADH:ubiquinone reductase</topic><topic>Naphthoquinones - metabolism</topic><topic>Oxidation-Reduction</topic><topic>Quinone Reductases - metabolism</topic><topic>Rotenone - pharmacology</topic><topic>Steady-state kinetics</topic><topic>TN/K m</topic><topic>turnover number</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Čénas, Narimantas K.</creatorcontrib><creatorcontrib>Bironaité, Daiva A.</creatorcontrib><creatorcontrib>Kulys, Juozas J.</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>Čénas, Narimantas K.</au><au>Bironaité, Daiva A.</au><au>Kulys, Juozas J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>On the mechanism of rotenone-insensitive reduction of quinones by mitochondrial NADH:ubiquinone reductase The high affinity binding of NAD + and NADH to the reduced enzyme form</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1991-06-24</date><risdate>1991</risdate><volume>284</volume><issue>2</issue><spage>192</spage><epage>194</epage><pages>192-194</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>NADH acts as an incomplete competitive inhibitor for 5,8-dioxy-1,4-naphtoquinone during its rotenone-insensitive reduction by mitochondrial NADH:ubiquinone reductase. NAD
+ and ADP-ribose act as incomplete mixed-type inhibitors.
K
i of NAD
+ and NADH towards quinone are about one order less than towards ferricyanide. The bimolecular rate constant of the reduction of the enzyme by NADH in the quinone reductase reaction is about 2 times less than that of ferricyanide reductase reaction. These data indicate that the reduction site of 5,8-dioxy-1,4-naphtoquinone is close to NAD
+/NADH and ferricyanide binding site. It seems that during the steady-state reduction of ferricyanide and 5,8-dioxy-1,4-naphtoquinone these oxidizers react with NADH:ubiquinone reductase reduced to different extents.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>1905649</pmid><doi>10.1016/0014-5793(91)80682-S</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1991-06, Vol.284 (2), p.192-194 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_80656534 |
| source | MEDLINE; Elsevier ScienceDirect Journals; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Animals Binding, Competitive biomolecular rate constant Cattle Electron acceptor Mitochondria, Heart - enzymology NAD - metabolism NAD(P)H Dehydrogenase (Quinone) NADH:ubiquinone reductase Naphthoquinones - metabolism Oxidation-Reduction Quinone Reductases - metabolism Rotenone - pharmacology Steady-state kinetics TN/K m turnover number |
| title | On the mechanism of rotenone-insensitive reduction of quinones by mitochondrial NADH:ubiquinone reductase The high affinity binding of NAD + and NADH to the reduced enzyme form |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-29T17%3A38%3A27IST&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=On%20the%20mechanism%20of%20rotenone-insensitive%20reduction%20of%20quinones%20by%20mitochondrial%20NADH:ubiquinone%20reductase%20The%20high%20affinity%20binding%20of%20NAD%20+%20and%20NADH%20to%20the%20reduced%20enzyme%20form&rft.jtitle=FEBS%20letters&rft.au=%C4%8C%C3%A9nas,%20Narimantas%20K.&rft.date=1991-06-24&rft.volume=284&rft.issue=2&rft.spage=192&rft.epage=194&rft.pages=192-194&rft.issn=0014-5793&rft.eissn=1873-3468&rft_id=info:doi/10.1016/0014-5793(91)80682-S&rft_dat=%3Cproquest_cross%3E80656534%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=80656534&rft_id=info:pmid/1905649&rft_els_id=001457939180682S&rfr_iscdi=true |