Reduction of cytochrome b-561 through the antimycin-sensitive site of the ubiquinol-cytochrome c2 oxidoreductase complex of Rhodopseudomonas sphaeroides
Cytochrome b-561 of the ubiquinol-cytochrome c 2 oxidoreductase complex of Rhodopseudomonas sphaeroides is reduced after flash illumination in the presence of myxothiazol in an antimycin-sensitive reaction. Flash-induced reduction was observed over the redox range in which cytochrome b-561 and the Q...
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| Veröffentlicht in: | FEBS letters 1984-12, Vol.178 (2), p.336-342 |
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| creator | Glaser, Elzbieta G. Meinhardt, Steven W. Crofts, Antony R. |
| description | Cytochrome
b-561 of the ubiquinol-cytochrome
c
2 oxidoreductase complex of
Rhodopseudomonas sphaeroides is reduced after flash illumination in the presence of myxothiazol in an antimycin-sensitive reaction. Flash-induced reduction was observed over the redox range in which cytochrome
b-561 and the Q-pool are both oxidized before the flash. The extent of reduction increased with increasing pH, and was maximal at pH > 10.0 where the extent approached that observed in the presence of antimycin following a group of flashes. Reduction of cytochrome
b-561 in the presence of myxothiazol showed a lag of ~ 1 ms after the flash, followed by reduction with (
t
1
2
~ 6 ms; by analogy with the similar kinetics of the quinol oxidase site, we suggest that the rate is determined by collision with the QH
2 produced in the pool on flash excitation. |
| doi_str_mv | 10.1016/0014-5793(84)80629-8 |
| format | Article |
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b-561 of the ubiquinol-cytochrome
c
2 oxidoreductase complex of
Rhodopseudomonas sphaeroides is reduced after flash illumination in the presence of myxothiazol in an antimycin-sensitive reaction. Flash-induced reduction was observed over the redox range in which cytochrome
b-561 and the Q-pool are both oxidized before the flash. The extent of reduction increased with increasing pH, and was maximal at pH > 10.0 where the extent approached that observed in the presence of antimycin following a group of flashes. Reduction of cytochrome
b-561 in the presence of myxothiazol showed a lag of ~ 1 ms after the flash, followed by reduction with (
t
1
2
~ 6 ms; by analogy with the similar kinetics of the quinol oxidase site, we suggest that the rate is determined by collision with the QH
2 produced in the pool on flash excitation.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(84)80629-8</identifier><identifier>PMID: 6096171</identifier><identifier>CODEN: FEBLAL</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Analytical, structural and metabolic biochemistry ; Antimycin A - pharmacology ; Antimycin-sensitivity ; Bacterial Chromatophores - enzymology ; Biological and medical sciences ; Cytochrome b Group - metabolism ; Cytochrome b-561 ; Electrogenic process ; Electron Transport Complex III ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Hydrogen-Ion Concentration ; Kinetics ; Light ; Methacrylates ; Multienzyme Complexes - metabolism ; Multienzyme Complexes - radiation effects ; Myxothiazol ; NADH, NADPH Oxidoreductases - metabolism ; Oxidation-Reduction ; Oxidoreductases ; Quinone Reductases - metabolism ; Quinone Reductases - radiation effects ; Rhodobacter sphaeroides - enzymology ; Rps. sphaeroides ; Spectrophotometry ; Spheroplasts - enzymology ; Thiazoles - pharmacology ; Ubiquinol-cytochrome c 2 oxidoreductase</subject><ispartof>FEBS letters, 1984-12, Vol.178 (2), p.336-342</ispartof><rights>1984</rights><rights>1985 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(84)80629-8$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,778,782,3539,27907,27908,45978</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=9220578$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6096171$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Glaser, Elzbieta G.</creatorcontrib><creatorcontrib>Meinhardt, Steven W.</creatorcontrib><creatorcontrib>Crofts, Antony R.</creatorcontrib><title>Reduction of cytochrome b-561 through the antimycin-sensitive site of the ubiquinol-cytochrome c2 oxidoreductase complex of Rhodopseudomonas sphaeroides</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Cytochrome
b-561 of the ubiquinol-cytochrome
c
2 oxidoreductase complex of
Rhodopseudomonas sphaeroides is reduced after flash illumination in the presence of myxothiazol in an antimycin-sensitive reaction. Flash-induced reduction was observed over the redox range in which cytochrome
b-561 and the Q-pool are both oxidized before the flash. The extent of reduction increased with increasing pH, and was maximal at pH > 10.0 where the extent approached that observed in the presence of antimycin following a group of flashes. Reduction of cytochrome
b-561 in the presence of myxothiazol showed a lag of ~ 1 ms after the flash, followed by reduction with (
t
1
2
~ 6 ms; by analogy with the similar kinetics of the quinol oxidase site, we suggest that the rate is determined by collision with the QH
2 produced in the pool on flash excitation.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Antimycin A - pharmacology</subject><subject>Antimycin-sensitivity</subject><subject>Bacterial Chromatophores - enzymology</subject><subject>Biological and medical sciences</subject><subject>Cytochrome b Group - metabolism</subject><subject>Cytochrome b-561</subject><subject>Electrogenic process</subject><subject>Electron Transport Complex III</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Light</subject><subject>Methacrylates</subject><subject>Multienzyme Complexes - metabolism</subject><subject>Multienzyme Complexes - radiation effects</subject><subject>Myxothiazol</subject><subject>NADH, NADPH Oxidoreductases - metabolism</subject><subject>Oxidation-Reduction</subject><subject>Oxidoreductases</subject><subject>Quinone Reductases - metabolism</subject><subject>Quinone Reductases - radiation effects</subject><subject>Rhodobacter sphaeroides - enzymology</subject><subject>Rps. sphaeroides</subject><subject>Spectrophotometry</subject><subject>Spheroplasts - enzymology</subject><subject>Thiazoles - pharmacology</subject><subject>Ubiquinol-cytochrome c 2 oxidoreductase</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNUdFqFTEQDaLUa_UPFPZBRB9Sk81ukn0RpKgVCkKpzyE7mfVGdpNtslt6_8TPNdteSp8OM-fMGWYOIW85O-OMy8-M8Ya2qhMfdfNJM1l3VD8jO66VoKKR-jnZPUpeklc5_2Wl1rw7ISeSdZIrviP_rtCtsPgYqjhUcFgi7FOcsOppK3m1lGL9sy-IlQ2Lnw7gA80Ysl_8LVYFcBvc-LX3N6sPcaRPbKCu4p13Md2vsbl04jSPeLdNXe2ji3PG1cUpBpurPO8tpugd5tfkxWDHjG-OeEp-f_92fX5BL3_9-Hn-9ZKiEHKhne1QOQZWsAFdb53ooJODBMl7YLVjEtGp2glRtwNC2wyg20E5oTQCWC1OyYcH3znFmxXzYiafAcfRBoxrNqrVrFWtKsJ3R-HaT-jMnPxk08EcX1n490feZrDjkGwAnx9lXV0Xn23flwcZlqNuPSaTwWMAdD4hLMZFbzgzW8Jmi89s8RndmPuEjRb_AeavnE8</recordid><startdate>19841210</startdate><enddate>19841210</enddate><creator>Glaser, Elzbieta G.</creator><creator>Meinhardt, Steven W.</creator><creator>Crofts, Antony R.</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19841210</creationdate><title>Reduction of cytochrome b-561 through the antimycin-sensitive site of the ubiquinol-cytochrome c2 oxidoreductase complex of Rhodopseudomonas sphaeroides</title><author>Glaser, Elzbieta G. ; Meinhardt, Steven W. ; Crofts, Antony R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e336t-9a9e7d0ca30fedbad39c96f6c61bc02d06eed72d3325fec54fc85f7d378ecca83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Antimycin A - pharmacology</topic><topic>Antimycin-sensitivity</topic><topic>Bacterial Chromatophores - enzymology</topic><topic>Biological and medical sciences</topic><topic>Cytochrome b Group - metabolism</topic><topic>Cytochrome b-561</topic><topic>Electrogenic process</topic><topic>Electron Transport Complex III</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Light</topic><topic>Methacrylates</topic><topic>Multienzyme Complexes - metabolism</topic><topic>Multienzyme Complexes - radiation effects</topic><topic>Myxothiazol</topic><topic>NADH, NADPH Oxidoreductases - metabolism</topic><topic>Oxidation-Reduction</topic><topic>Oxidoreductases</topic><topic>Quinone Reductases - metabolism</topic><topic>Quinone Reductases - radiation effects</topic><topic>Rhodobacter sphaeroides - enzymology</topic><topic>Rps. sphaeroides</topic><topic>Spectrophotometry</topic><topic>Spheroplasts - enzymology</topic><topic>Thiazoles - pharmacology</topic><topic>Ubiquinol-cytochrome c 2 oxidoreductase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Glaser, Elzbieta G.</creatorcontrib><creatorcontrib>Meinhardt, Steven W.</creatorcontrib><creatorcontrib>Crofts, Antony R.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Glaser, Elzbieta G.</au><au>Meinhardt, Steven W.</au><au>Crofts, Antony R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Reduction of cytochrome b-561 through the antimycin-sensitive site of the ubiquinol-cytochrome c2 oxidoreductase complex of Rhodopseudomonas sphaeroides</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1984-12-10</date><risdate>1984</risdate><volume>178</volume><issue>2</issue><spage>336</spage><epage>342</epage><pages>336-342</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>Cytochrome
b-561 of the ubiquinol-cytochrome
c
2 oxidoreductase complex of
Rhodopseudomonas sphaeroides is reduced after flash illumination in the presence of myxothiazol in an antimycin-sensitive reaction. Flash-induced reduction was observed over the redox range in which cytochrome
b-561 and the Q-pool are both oxidized before the flash. The extent of reduction increased with increasing pH, and was maximal at pH > 10.0 where the extent approached that observed in the presence of antimycin following a group of flashes. Reduction of cytochrome
b-561 in the presence of myxothiazol showed a lag of ~ 1 ms after the flash, followed by reduction with (
t
1
2
~ 6 ms; by analogy with the similar kinetics of the quinol oxidase site, we suggest that the rate is determined by collision with the QH
2 produced in the pool on flash excitation.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>6096171</pmid><doi>10.1016/0014-5793(84)80629-8</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1984-12, Vol.178 (2), p.336-342 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_75805757 |
| source | Elsevier ScienceDirect Journals Complete - AutoHoldings; MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Analytical, structural and metabolic biochemistry Antimycin A - pharmacology Antimycin-sensitivity Bacterial Chromatophores - enzymology Biological and medical sciences Cytochrome b Group - metabolism Cytochrome b-561 Electrogenic process Electron Transport Complex III Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Kinetics Light Methacrylates Multienzyme Complexes - metabolism Multienzyme Complexes - radiation effects Myxothiazol NADH, NADPH Oxidoreductases - metabolism Oxidation-Reduction Oxidoreductases Quinone Reductases - metabolism Quinone Reductases - radiation effects Rhodobacter sphaeroides - enzymology Rps. sphaeroides Spectrophotometry Spheroplasts - enzymology Thiazoles - pharmacology Ubiquinol-cytochrome c 2 oxidoreductase |
| title | Reduction of cytochrome b-561 through the antimycin-sensitive site of the ubiquinol-cytochrome c2 oxidoreductase complex of Rhodopseudomonas sphaeroides |
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