Electrogenic proton transfer in Rhodobacter sphaeroides reaction centers: effect of coenzyme Q(10) substitution by decylubiquinone in the Q(B) binding site
An electrometric technique was used to investigate the effect of coenzyme Q(10) (UQ), substitution by decylubiquinone (dQ) at the Q(B) binding site of reaction centers (UQ-RC and dQ-RC, respectively) on the electrogenic proton transfer kinetics upon Q(B) reduction in Rhodobacter sphaeroides chromato...
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| Veröffentlicht in: | FEBS letters 2001-06, Vol.499 (1-2), p.116-120 |
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| creator | Gopta, O A Semenov, A Y Bloch, D A |
| description | An electrometric technique was used to investigate the effect of coenzyme Q(10) (UQ), substitution by decylubiquinone (dQ) at the Q(B) binding site of reaction centers (UQ-RC and dQ-RC, respectively) on the electrogenic proton transfer kinetics upon Q(B) reduction in Rhodobacter sphaeroides chromatophores. Unlike dQ-RC, the kinetics of the second flash-induced proton uptake in UQ-RC clearly deviated from the mono-exponential one. The activation energy (about 30 kJ/mol) and the pH profile of the kinetics in dQ-RC were similar to those in UQ-RC, with the power law approximation used in the latter case. The interpretation of the data presumed the quinone translocation between the two binding positions within the Q(B) site. It is proposed that the native isoprenyl side chain (in contrast to decyl chain) favors the equilibrium binding of neutral quinone at the redox-active 'proximal' position, but causes a higher barrier for the hydroquinone movement from 'proximal' to 'distal' position. |
| doi_str_mv | 10.1016/S0014-5793(01)02537-6 |
| format | Article |
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Unlike dQ-RC, the kinetics of the second flash-induced proton uptake in UQ-RC clearly deviated from the mono-exponential one. The activation energy (about 30 kJ/mol) and the pH profile of the kinetics in dQ-RC were similar to those in UQ-RC, with the power law approximation used in the latter case. The interpretation of the data presumed the quinone translocation between the two binding positions within the Q(B) site. It is proposed that the native isoprenyl side chain (in contrast to decyl chain) favors the equilibrium binding of neutral quinone at the redox-active 'proximal' position, but causes a higher barrier for the hydroquinone movement from 'proximal' to 'distal' position.</description><identifier>ISSN: 0014-5793</identifier><identifier>DOI: 10.1016/S0014-5793(01)02537-6</identifier><identifier>PMID: 11418124</identifier><language>eng</language><publisher>England</publisher><subject>Bacterial Chromatophores - chemistry ; Bacterial Chromatophores - metabolism ; Binding Sites ; Coenzymes ; Hydrogen-Ion Concentration ; Kinetics ; Protons ; Rhodobacter sphaeroides - chemistry ; Rhodobacter sphaeroides - metabolism ; Temperature ; Thermodynamics ; Ubiquinone - analogs & derivatives ; Ubiquinone - metabolism</subject><ispartof>FEBS letters, 2001-06, Vol.499 (1-2), p.116-120</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11418124$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gopta, O A</creatorcontrib><creatorcontrib>Semenov, A Y</creatorcontrib><creatorcontrib>Bloch, D A</creatorcontrib><title>Electrogenic proton transfer in Rhodobacter sphaeroides reaction centers: effect of coenzyme Q(10) substitution by decylubiquinone in the Q(B) binding site</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>An electrometric technique was used to investigate the effect of coenzyme Q(10) (UQ), substitution by decylubiquinone (dQ) at the Q(B) binding site of reaction centers (UQ-RC and dQ-RC, respectively) on the electrogenic proton transfer kinetics upon Q(B) reduction in Rhodobacter sphaeroides chromatophores. Unlike dQ-RC, the kinetics of the second flash-induced proton uptake in UQ-RC clearly deviated from the mono-exponential one. The activation energy (about 30 kJ/mol) and the pH profile of the kinetics in dQ-RC were similar to those in UQ-RC, with the power law approximation used in the latter case. The interpretation of the data presumed the quinone translocation between the two binding positions within the Q(B) site. It is proposed that the native isoprenyl side chain (in contrast to decyl chain) favors the equilibrium binding of neutral quinone at the redox-active 'proximal' position, but causes a higher barrier for the hydroquinone movement from 'proximal' to 'distal' position.</description><subject>Bacterial Chromatophores - chemistry</subject><subject>Bacterial Chromatophores - metabolism</subject><subject>Binding Sites</subject><subject>Coenzymes</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Protons</subject><subject>Rhodobacter sphaeroides - chemistry</subject><subject>Rhodobacter sphaeroides - metabolism</subject><subject>Temperature</subject><subject>Thermodynamics</subject><subject>Ubiquinone - analogs & derivatives</subject><subject>Ubiquinone - metabolism</subject><issn>0014-5793</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kMtOwzAQRb0A0VL4BJBXqF0E_MjL7KAqD6kS4rWuYmfcGqV2GzuL8Cv8LC4UVjNz5-iO5iJ0RsklJTS_eiWEpklWCD4mdEJYxoskP0DDf3mAjr3_IHEuqThCA0rT2LF0iL5mDajQuiVYo_CmdcFZHNrKeg0tNha_rFztZKVCHP1mVUHrTA0etxA1E2EFNu78NQatoxV2GisH9rNfA34eUzLBvpM-mND94LLHNai-6aTZdsY6C7srYbWDbydYGlsbu8TeBDhBh7pqPJzu6wi9383epg_J_On-cXozTzaUi5DkLMtFLYWuUyiVVHmuieKCZ6TSBSkZ5UzKkpVZnknNYhykzDhLKSVlIUpe8xG6-PWN72878GGxNl5B01QWXOcXBREpzwSL4Pke7OQa6sWmNeuq7Rd_cfJvjP53mQ</recordid><startdate>20010615</startdate><enddate>20010615</enddate><creator>Gopta, O A</creator><creator>Semenov, A Y</creator><creator>Bloch, D A</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>20010615</creationdate><title>Electrogenic proton transfer in Rhodobacter sphaeroides reaction centers: effect of coenzyme Q(10) substitution by decylubiquinone in the Q(B) binding site</title><author>Gopta, O A ; Semenov, A Y ; Bloch, D A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p139t-62569db9fd4e8cbc66f0c39350af7082132bb828565bf257908532411087983d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Bacterial Chromatophores - chemistry</topic><topic>Bacterial Chromatophores - metabolism</topic><topic>Binding Sites</topic><topic>Coenzymes</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Protons</topic><topic>Rhodobacter sphaeroides - chemistry</topic><topic>Rhodobacter sphaeroides - metabolism</topic><topic>Temperature</topic><topic>Thermodynamics</topic><topic>Ubiquinone - analogs & derivatives</topic><topic>Ubiquinone - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gopta, O A</creatorcontrib><creatorcontrib>Semenov, A Y</creatorcontrib><creatorcontrib>Bloch, D A</creatorcontrib><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>Gopta, O A</au><au>Semenov, A Y</au><au>Bloch, D A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Electrogenic proton transfer in Rhodobacter sphaeroides reaction centers: effect of coenzyme Q(10) substitution by decylubiquinone in the Q(B) binding site</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2001-06-15</date><risdate>2001</risdate><volume>499</volume><issue>1-2</issue><spage>116</spage><epage>120</epage><pages>116-120</pages><issn>0014-5793</issn><abstract>An electrometric technique was used to investigate the effect of coenzyme Q(10) (UQ), substitution by decylubiquinone (dQ) at the Q(B) binding site of reaction centers (UQ-RC and dQ-RC, respectively) on the electrogenic proton transfer kinetics upon Q(B) reduction in Rhodobacter sphaeroides chromatophores. Unlike dQ-RC, the kinetics of the second flash-induced proton uptake in UQ-RC clearly deviated from the mono-exponential one. The activation energy (about 30 kJ/mol) and the pH profile of the kinetics in dQ-RC were similar to those in UQ-RC, with the power law approximation used in the latter case. The interpretation of the data presumed the quinone translocation between the two binding positions within the Q(B) site. It is proposed that the native isoprenyl side chain (in contrast to decyl chain) favors the equilibrium binding of neutral quinone at the redox-active 'proximal' position, but causes a higher barrier for the hydroquinone movement from 'proximal' to 'distal' position.</abstract><cop>England</cop><pmid>11418124</pmid><doi>10.1016/S0014-5793(01)02537-6</doi><tpages>5</tpages></addata></record> |
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| ispartof | FEBS letters, 2001-06, Vol.499 (1-2), p.116-120 |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Wiley Online Library Free Content; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Bacterial Chromatophores - chemistry Bacterial Chromatophores - metabolism Binding Sites Coenzymes Hydrogen-Ion Concentration Kinetics Protons Rhodobacter sphaeroides - chemistry Rhodobacter sphaeroides - metabolism Temperature Thermodynamics Ubiquinone - analogs & derivatives Ubiquinone - metabolism |
| title | Electrogenic proton transfer in Rhodobacter sphaeroides reaction centers: effect of coenzyme Q(10) substitution by decylubiquinone in the Q(B) binding site |
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