Antimycin inhibition of the cytochrome bd complex from Azotobacter vinelandii indicates the presence of a branched electron transfer pathway for the oxidation of ubiquinol
Antimycin A and UHBDT inhibit the activity of the purified cytochrome bd complex from Azotobacter vinelandii. Inhibition of activity is non-competitive and antimycin A binding induces a shift to the red in the spectrum of a b-type haem. No inhibitory effects were seen with myxothiazol. Steady-state...
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| Veröffentlicht in: | FEBS letters 1994-05, Vol.345 (2), p.198-202 |
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| creator | Jünemann, Susanne Wrigglesworth, John M. |
| description | Antimycin A and UHBDT inhibit the activity of the purified cytochrome
bd complex from
Azotobacter vinelandii. Inhibition of activity is non-competitive and antimycin A binding induces a shift to the red in the spectrum of a
b-type haem. No inhibitory effects were seen with myxothiazol. Steady-state experiments indicate that the site of inhibition for antimycin A lies on the low-potential side of haem
b
558. In the presence of antimycin A at concentrations sufficient to inhibit respiration, some direct electron transfer from ubiquinol-1 to haem
b
595 and haem
d still occurs. The results are consistent with a branched electron transfer pathway from ubiquinol to the oxygen reduction site. |
| doi_str_mv | 10.1016/0014-5793(94)00372-6 |
| format | Article |
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bd complex from
Azotobacter vinelandii. Inhibition of activity is non-competitive and antimycin A binding induces a shift to the red in the spectrum of a
b-type haem. No inhibitory effects were seen with myxothiazol. Steady-state experiments indicate that the site of inhibition for antimycin A lies on the low-potential side of haem
b
558. In the presence of antimycin A at concentrations sufficient to inhibit respiration, some direct electron transfer from ubiquinol-1 to haem
b
595 and haem
d still occurs. The results are consistent with a branched electron transfer pathway from ubiquinol to the oxygen reduction site.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(94)00372-6</identifier><identifier>PMID: 8200455</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Antimycin A ; Antimycin A - pharmacology ; Azotobacter vinelandii ; Azotobacter vinelandii - enzymology ; Cytochrome bd ; Cytochromes - antagonists & inhibitors ; Cytochromes - isolation & purification ; Cytochromes - metabolism ; Dithiothreitol - pharmacology ; DTT, dithiothreitol ; Electron Transport ; Electron Transport Chain Complex Proteins ; Escherichia coli Proteins ; Kinetics ; Methacrylates ; Oxidation-Reduction ; Oxidoreductases - antagonists & inhibitors ; Oxidoreductases - isolation & purification ; Oxidoreductases - metabolism ; Thiazoles - pharmacology ; TMPD, N,N,N′,N′-tetramethyl-p-phenylenediamine ; Ubiquinone - analogs & derivatives ; Ubiquinone - metabolism ; UHDBT, undecylhydroxydioxobenzothiazole</subject><ispartof>FEBS letters, 1994-05, Vol.345 (2), p.198-202</ispartof><rights>1994</rights><rights>FEBS Letters 345 (1994) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4976-256a95b89f96bb8f975fba41deebca43211314cf305b30025c60e7593549fd083</citedby><cites>FETCH-LOGICAL-c4976-256a95b89f96bb8f975fba41deebca43211314cf305b30025c60e7593549fd083</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(94)00372-6$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8200455$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jünemann, Susanne</creatorcontrib><creatorcontrib>Wrigglesworth, John M.</creatorcontrib><title>Antimycin inhibition of the cytochrome bd complex from Azotobacter vinelandii indicates the presence of a branched electron transfer pathway for the oxidation of ubiquinol</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Antimycin A and UHBDT inhibit the activity of the purified cytochrome
bd complex from
Azotobacter vinelandii. Inhibition of activity is non-competitive and antimycin A binding induces a shift to the red in the spectrum of a
b-type haem. No inhibitory effects were seen with myxothiazol. Steady-state experiments indicate that the site of inhibition for antimycin A lies on the low-potential side of haem
b
558. In the presence of antimycin A at concentrations sufficient to inhibit respiration, some direct electron transfer from ubiquinol-1 to haem
b
595 and haem
d still occurs. The results are consistent with a branched electron transfer pathway from ubiquinol to the oxygen reduction site.</description><subject>Antimycin A</subject><subject>Antimycin A - pharmacology</subject><subject>Azotobacter vinelandii</subject><subject>Azotobacter vinelandii - enzymology</subject><subject>Cytochrome bd</subject><subject>Cytochromes - antagonists & inhibitors</subject><subject>Cytochromes - isolation & purification</subject><subject>Cytochromes - metabolism</subject><subject>Dithiothreitol - pharmacology</subject><subject>DTT, dithiothreitol</subject><subject>Electron Transport</subject><subject>Electron Transport Chain Complex Proteins</subject><subject>Escherichia coli Proteins</subject><subject>Kinetics</subject><subject>Methacrylates</subject><subject>Oxidation-Reduction</subject><subject>Oxidoreductases - antagonists & inhibitors</subject><subject>Oxidoreductases - isolation & purification</subject><subject>Oxidoreductases - metabolism</subject><subject>Thiazoles - pharmacology</subject><subject>TMPD, N,N,N′,N′-tetramethyl-p-phenylenediamine</subject><subject>Ubiquinone - analogs & derivatives</subject><subject>Ubiquinone - metabolism</subject><subject>UHDBT, undecylhydroxydioxobenzothiazole</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNUc1u1DAYjBCoLIU3AMknRA8BO7Gd-IK0VF1AqsQFzpbtfFaMkji1vW3DK_GSdXaXHoGT5flm5vuZonhN8HuCCf-AMaEla0T9TtALjOumKvmTYkPapi5rytunxeaR8rx4EeNPnP8tEWfFWVthTBnbFL-3U3LjYtyE3NQ77ZLzE_IWpR6QWZI3ffAjIN0h48d5gHtkM4C2v3zyWpkEAd26CQY1dc5lj84ZlSAe9HOACJOB1U8hHdRkeugQDGBSyG1SRqLNDrNK_Z1akPXhIPT3rlN_Jtlrd7N3kx9eFs-sGiK8Or3nxY_d1ffLL-X1t89fL7fXpaGi4WXFuBJMt8IKrnVrRcOsVpR0ANooWleE1IQaW2Oma4wrZjiGhomaUWE73Nbnxduj7xz8zR5ikqOLBoa8I_h9lA1nROB85n8RCee44lxkIj0STfAxBrByDm5UYZEEyzVMuSYl16SkoPIQpuRZ9ubkv9cjdI-iU3q5vjvW79wAy395yt3Vp2otrLigB3Rt9PFoBPmstw6CjMatyXUu5Kxk593fJ30AZbPE_Q</recordid><startdate>19940530</startdate><enddate>19940530</enddate><creator>Jünemann, Susanne</creator><creator>Wrigglesworth, John M.</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19940530</creationdate><title>Antimycin inhibition of the cytochrome bd complex from Azotobacter vinelandii indicates the presence of a branched electron transfer pathway for the oxidation of ubiquinol</title><author>Jünemann, Susanne ; Wrigglesworth, John M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4976-256a95b89f96bb8f975fba41deebca43211314cf305b30025c60e7593549fd083</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Antimycin A</topic><topic>Antimycin A - pharmacology</topic><topic>Azotobacter vinelandii</topic><topic>Azotobacter vinelandii - enzymology</topic><topic>Cytochrome bd</topic><topic>Cytochromes - antagonists & inhibitors</topic><topic>Cytochromes - isolation & purification</topic><topic>Cytochromes - metabolism</topic><topic>Dithiothreitol - pharmacology</topic><topic>DTT, dithiothreitol</topic><topic>Electron Transport</topic><topic>Electron Transport Chain Complex Proteins</topic><topic>Escherichia coli Proteins</topic><topic>Kinetics</topic><topic>Methacrylates</topic><topic>Oxidation-Reduction</topic><topic>Oxidoreductases - antagonists & inhibitors</topic><topic>Oxidoreductases - isolation & purification</topic><topic>Oxidoreductases - metabolism</topic><topic>Thiazoles - pharmacology</topic><topic>TMPD, N,N,N′,N′-tetramethyl-p-phenylenediamine</topic><topic>Ubiquinone - analogs & derivatives</topic><topic>Ubiquinone - metabolism</topic><topic>UHDBT, undecylhydroxydioxobenzothiazole</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jünemann, Susanne</creatorcontrib><creatorcontrib>Wrigglesworth, John M.</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jünemann, Susanne</au><au>Wrigglesworth, John M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Antimycin inhibition of the cytochrome bd complex from Azotobacter vinelandii indicates the presence of a branched electron transfer pathway for the oxidation of ubiquinol</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1994-05-30</date><risdate>1994</risdate><volume>345</volume><issue>2</issue><spage>198</spage><epage>202</epage><pages>198-202</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Antimycin A and UHBDT inhibit the activity of the purified cytochrome
bd complex from
Azotobacter vinelandii. Inhibition of activity is non-competitive and antimycin A binding induces a shift to the red in the spectrum of a
b-type haem. No inhibitory effects were seen with myxothiazol. Steady-state experiments indicate that the site of inhibition for antimycin A lies on the low-potential side of haem
b
558. In the presence of antimycin A at concentrations sufficient to inhibit respiration, some direct electron transfer from ubiquinol-1 to haem
b
595 and haem
d still occurs. The results are consistent with a branched electron transfer pathway from ubiquinol to the oxygen reduction site.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>8200455</pmid><doi>10.1016/0014-5793(94)00372-6</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1994-05, Vol.345 (2), p.198-202 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76519087 |
| source | MEDLINE; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Antimycin A Antimycin A - pharmacology Azotobacter vinelandii Azotobacter vinelandii - enzymology Cytochrome bd Cytochromes - antagonists & inhibitors Cytochromes - isolation & purification Cytochromes - metabolism Dithiothreitol - pharmacology DTT, dithiothreitol Electron Transport Electron Transport Chain Complex Proteins Escherichia coli Proteins Kinetics Methacrylates Oxidation-Reduction Oxidoreductases - antagonists & inhibitors Oxidoreductases - isolation & purification Oxidoreductases - metabolism Thiazoles - pharmacology TMPD, N,N,N′,N′-tetramethyl-p-phenylenediamine Ubiquinone - analogs & derivatives Ubiquinone - metabolism UHDBT, undecylhydroxydioxobenzothiazole |
| title | Antimycin inhibition of the cytochrome bd complex from Azotobacter vinelandii indicates the presence of a branched electron transfer pathway for the oxidation of ubiquinol |
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