An inhibitory high affinity binding site for ADP in the oligomycin-sensitive ATPase of beef heart submitochondrial particles
Kinetic evidence are presented for the existence of a high affinity inhibitory site for ADP /K i < 10 −7 M/ in the oligomycin-sensitive ATPase of beef heart submitochondrial particles. The ATPase·ADP complex is completely inactive in the ATPase reaction; it can be converted into active ATPase in...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1979, Vol.86 (2), p.434-439 |
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| container_issue | 2 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Fitin, A.F. Vasilyeva, E.A. Vinogradov, A.D. |
| description | Kinetic evidence are presented for the existence of a high affinity inhibitory site for ADP /K
i < 10
−7 M/ in the oligomycin-sensitive ATPase of beef heart submitochondrial particles. The ATPase·ADP complex is completely inactive in the ATPase reaction; it can be converted into active ATPase in a slow ATP-dependent reaction. The dependence of a first order rate constant for activation of the enzyme·ADP complex on concentration of ATP gives a K
m value equal to that for ATP in the ATPase reaction. The data obtained suggest that the membrane-bound ATPase complex contains two kinetically distinct nucleotide-binding centers, i.e. center 1 binds ATP or ADP with a formation of enzyme-substrate or enzyme-competitive inhibitor complexes: center 2 binds ADP with a formation of a complex which is able to bind ATP in center 1 and unable to hydrolyze the bound ATP. The binding of ATP or ADP in center 1 changes the reactivity of center 2 towards ADP. |
| doi_str_mv | 10.1016/0006-291X(79)90884-2 |
| format | Article |
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−7 M/ in the oligomycin-sensitive ATPase of beef heart submitochondrial particles. The ATPase·ADP complex is completely inactive in the ATPase reaction; it can be converted into active ATPase in a slow ATP-dependent reaction. The dependence of a first order rate constant for activation of the enzyme·ADP complex on concentration of ATP gives a K
m value equal to that for ATP in the ATPase reaction. The data obtained suggest that the membrane-bound ATPase complex contains two kinetically distinct nucleotide-binding centers, i.e. center 1 binds ATP or ADP with a formation of enzyme-substrate or enzyme-competitive inhibitor complexes: center 2 binds ADP with a formation of a complex which is able to bind ATP in center 1 and unable to hydrolyze the bound ATP. The binding of ATP or ADP in center 1 changes the reactivity of center 2 towards ADP.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(79)90884-2</identifier><identifier>PMID: 154889</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adenosine Diphosphate - metabolism ; Adenosine Triphosphatases - metabolism ; Animals ; Binding Sites ; Cattle ; Kinetics ; Mitochondria - enzymology ; Mitochondria, Heart - enzymology ; Oligomycins - pharmacology ; Submitochondrial Particles - enzymology</subject><ispartof>Biochemical and biophysical research communications, 1979, Vol.86 (2), p.434-439</ispartof><rights>1979</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c317t-6ce2645e8f1b08c24190d500026e86d44f89b039e67307c41fb62e75b686c2db3</citedby><cites>FETCH-LOGICAL-c317t-6ce2645e8f1b08c24190d500026e86d44f89b039e67307c41fb62e75b686c2db3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0006-291X(79)90884-2$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,4022,27922,27923,27924,45994</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/154889$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fitin, A.F.</creatorcontrib><creatorcontrib>Vasilyeva, E.A.</creatorcontrib><creatorcontrib>Vinogradov, A.D.</creatorcontrib><creatorcontrib>Universidad Nacional Autonoma de Mexico, Mexico, DF. Facultad de Medicina Veterinaria y Zootecnia</creatorcontrib><creatorcontrib>Ecole Nationale Superieure Agronomique de Montpellier, 34 (France)</creatorcontrib><title>An inhibitory high affinity binding site for ADP in the oligomycin-sensitive ATPase of beef heart submitochondrial particles</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Kinetic evidence are presented for the existence of a high affinity inhibitory site for ADP /K
i < 10
−7 M/ in the oligomycin-sensitive ATPase of beef heart submitochondrial particles. The ATPase·ADP complex is completely inactive in the ATPase reaction; it can be converted into active ATPase in a slow ATP-dependent reaction. The dependence of a first order rate constant for activation of the enzyme·ADP complex on concentration of ATP gives a K
m value equal to that for ATP in the ATPase reaction. The data obtained suggest that the membrane-bound ATPase complex contains two kinetically distinct nucleotide-binding centers, i.e. center 1 binds ATP or ADP with a formation of enzyme-substrate or enzyme-competitive inhibitor complexes: center 2 binds ADP with a formation of a complex which is able to bind ATP in center 1 and unable to hydrolyze the bound ATP. The binding of ATP or ADP in center 1 changes the reactivity of center 2 towards ADP.</description><subject>Adenosine Diphosphate - metabolism</subject><subject>Adenosine Triphosphatases - metabolism</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Cattle</subject><subject>Kinetics</subject><subject>Mitochondria - enzymology</subject><subject>Mitochondria, Heart - enzymology</subject><subject>Oligomycins - pharmacology</subject><subject>Submitochondrial Particles - enzymology</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1979</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtrGzEURkXpy037D0LRqqSLaSWNrMemYNL0AYEGmkB3YkZz5bllLDnSOGDoj68ch3aXleB-537oHkJOOfvAGVcfGWOqEZb_OtP2vWXGyEY8IQvOLGsEZ_IpWfxDXpJXpfxmjHOp7AvynC-lMXZB_qwixThij3PKezrieqRdCBhx3tMe44BxTQvOQEPKdPX5qtJ0HoGmCddps_cYmwKxEngHdHV91ZWaBdoDBDpCl2dadv2mtvsxxSFjN9FtnaKfoLwmz0I3FXjz8J6Qmy8X1-ffmssfX7-fry4b33I9N8qDUHIJJvCeGS8kt2xY1tOEAqMGKYOxPWstKN0y7SUPvRKgl70yyouhb0_Iu2PvNqfbHZTZbbB4mKYuQtoVp-VSaC50BeUR9DmVkiG4bcZNl_eOM3dw7g5C3UGo09bdO3eirp0-9NdTYfi_dC-5xm-PceiS69YZi7v5ya22TEojlHgMaK0SvAKfjgBUS3cI2RWPED0MmMHPbkj4-A__AgBro4w</recordid><startdate>1979</startdate><enddate>1979</enddate><creator>Fitin, A.F.</creator><creator>Vasilyeva, E.A.</creator><creator>Vinogradov, A.D.</creator><general>Elsevier Inc</general><scope>FBQ</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>1979</creationdate><title>An inhibitory high affinity binding site for ADP in the oligomycin-sensitive ATPase of beef heart submitochondrial particles</title><author>Fitin, A.F. ; Vasilyeva, E.A. ; Vinogradov, A.D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c317t-6ce2645e8f1b08c24190d500026e86d44f89b039e67307c41fb62e75b686c2db3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1979</creationdate><topic>Adenosine Diphosphate - metabolism</topic><topic>Adenosine Triphosphatases - metabolism</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Cattle</topic><topic>Kinetics</topic><topic>Mitochondria - enzymology</topic><topic>Mitochondria, Heart - enzymology</topic><topic>Oligomycins - pharmacology</topic><topic>Submitochondrial Particles - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fitin, A.F.</creatorcontrib><creatorcontrib>Vasilyeva, E.A.</creatorcontrib><creatorcontrib>Vinogradov, A.D.</creatorcontrib><creatorcontrib>Universidad Nacional Autonoma de Mexico, Mexico, DF. Facultad de Medicina Veterinaria y Zootecnia</creatorcontrib><creatorcontrib>Ecole Nationale Superieure Agronomique de Montpellier, 34 (France)</creatorcontrib><collection>AGRIS</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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fitin, A.F.</au><au>Vasilyeva, E.A.</au><au>Vinogradov, A.D.</au><aucorp>Universidad Nacional Autonoma de Mexico, Mexico, DF. Facultad de Medicina Veterinaria y Zootecnia</aucorp><aucorp>Ecole Nationale Superieure Agronomique de Montpellier, 34 (France)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>An inhibitory high affinity binding site for ADP in the oligomycin-sensitive ATPase of beef heart submitochondrial particles</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1979</date><risdate>1979</risdate><volume>86</volume><issue>2</issue><spage>434</spage><epage>439</epage><pages>434-439</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Kinetic evidence are presented for the existence of a high affinity inhibitory site for ADP /K
i < 10
−7 M/ in the oligomycin-sensitive ATPase of beef heart submitochondrial particles. The ATPase·ADP complex is completely inactive in the ATPase reaction; it can be converted into active ATPase in a slow ATP-dependent reaction. The dependence of a first order rate constant for activation of the enzyme·ADP complex on concentration of ATP gives a K
m value equal to that for ATP in the ATPase reaction. The data obtained suggest that the membrane-bound ATPase complex contains two kinetically distinct nucleotide-binding centers, i.e. center 1 binds ATP or ADP with a formation of enzyme-substrate or enzyme-competitive inhibitor complexes: center 2 binds ADP with a formation of a complex which is able to bind ATP in center 1 and unable to hydrolyze the bound ATP. The binding of ATP or ADP in center 1 changes the reactivity of center 2 towards ADP.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>154889</pmid><doi>10.1016/0006-291X(79)90884-2</doi><tpages>6</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1979, Vol.86 (2), p.434-439 |
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| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Adenosine Diphosphate - metabolism Adenosine Triphosphatases - metabolism Animals Binding Sites Cattle Kinetics Mitochondria - enzymology Mitochondria, Heart - enzymology Oligomycins - pharmacology Submitochondrial Particles - enzymology |
| title | An inhibitory high affinity binding site for ADP in the oligomycin-sensitive ATPase of beef heart submitochondrial particles |
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