The H +/ATP coupling ratio of the ATP synthase from thiol-modulated chloroplasts and two cyanobacterial strains is four
In this paper the authors emphasise that the proton translocating ATP synthase from thiol-modulated chloroplasts and two cyanobacterial strains has a coupling ratio of 4 protons per ATP synthesised or hydrolysed. This ratio is determined by several thermodynamic studies at equilibrium between phosph...
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| Veröffentlicht in: | FEBS letters 1996-02, Vol.379 (3), p.309-313 |
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| creator | Van Walraven, Hendrika S. Strotmann, Heinrich Schwarz, Oliver Rumberg, Bernd |
| description | In this paper the authors emphasise that the proton translocating ATP synthase from thiol-modulated chloroplasts and two cyanobacterial strains has a coupling ratio of 4 protons per ATP synthesised or hydrolysed. This ratio is determined by several thermodynamic studies at equilibrium between phosphate potential (
ΔG
p) and proton gradient (
Δ
μ
H+
), and is confirmed by measurement of proton flux during ATP hydrolysis. Ratios lower than 4 H
+/ATP that have been published in the past have predominantly been determined with the oxidised chloroplast enzyme. Errors in these measurements will be discussed. |
| doi_str_mv | 10.1016/0014-5793(95)01536-1 |
| format | Article |
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ΔG
p) and proton gradient (
Δ
μ
H+
), and is confirmed by measurement of proton flux during ATP hydrolysis. Ratios lower than 4 H
+/ATP that have been published in the past have predominantly been determined with the oxidised chloroplast enzyme. Errors in these measurements will be discussed.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(95)01536-1</identifier><identifier>PMID: 8603713</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>ATP synthase, H ; Chloroplasts ; Chloroplasts - metabolism ; Cyanobacteria ; Cyanobacteria - enzymology ; Energy transduction ; Enzyme regulation ; H +/ATP ratio ; hydrophilic part of the ATP synthase (prefix C refers to chloroplasts) ; membrane-bound part of the ATP synthase ; N-(1-naphtyl)ethylenediamine ; NED ; phosphate potential ; proton electrochemical potential difference ; Proton gradient ; Proton translocation ; Proton-Translocating ATPases - metabolism ; standard free energy ; Thermodynamics ; ΔG p ; ΔG ′ 0 ; Δμ¯H</subject><ispartof>FEBS letters, 1996-02, Vol.379 (3), p.309-313</ispartof><rights>1996</rights><rights>FEBS Letters 379 (1996) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4861-32a8e522f778d671eeba2d213e932c6ef97b65c0221a91609d2812ad14f296283</citedby><cites>FETCH-LOGICAL-c4861-32a8e522f778d671eeba2d213e932c6ef97b65c0221a91609d2812ad14f296283</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2F0014-5793%2895%2901536-1$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0014579395015361$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,3537,27901,27902,45550,45551,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8603713$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Van Walraven, Hendrika S.</creatorcontrib><creatorcontrib>Strotmann, Heinrich</creatorcontrib><creatorcontrib>Schwarz, Oliver</creatorcontrib><creatorcontrib>Rumberg, Bernd</creatorcontrib><title>The H +/ATP coupling ratio of the ATP synthase from thiol-modulated chloroplasts and two cyanobacterial strains is four</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>In this paper the authors emphasise that the proton translocating ATP synthase from thiol-modulated chloroplasts and two cyanobacterial strains has a coupling ratio of 4 protons per ATP synthesised or hydrolysed. This ratio is determined by several thermodynamic studies at equilibrium between phosphate potential (
ΔG
p) and proton gradient (
Δ
μ
H+
), and is confirmed by measurement of proton flux during ATP hydrolysis. Ratios lower than 4 H
+/ATP that have been published in the past have predominantly been determined with the oxidised chloroplast enzyme. Errors in these measurements will be discussed.</description><subject>ATP synthase, H</subject><subject>Chloroplasts</subject><subject>Chloroplasts - metabolism</subject><subject>Cyanobacteria</subject><subject>Cyanobacteria - enzymology</subject><subject>Energy transduction</subject><subject>Enzyme regulation</subject><subject>H +/ATP ratio</subject><subject>hydrophilic part of the ATP synthase (prefix C refers to chloroplasts)</subject><subject>membrane-bound part of the ATP synthase</subject><subject>N-(1-naphtyl)ethylenediamine</subject><subject>NED</subject><subject>phosphate potential</subject><subject>proton electrochemical potential difference</subject><subject>Proton gradient</subject><subject>Proton translocation</subject><subject>Proton-Translocating ATPases - metabolism</subject><subject>standard free energy</subject><subject>Thermodynamics</subject><subject>ΔG p</subject><subject>ΔG ′ 0</subject><subject>Δμ¯H</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkEuLFDEUhYMoYzv6DxSyEkXKyaMqj40wDtOOMKCLdh3SyS07kqq0Scqm_71V080sxdXlnnPuSfgQek3JR0qouCKEtk0nNX-nu_eEdlw09AlaUSV5w1uhnqLVY-Q5elHKLzLviuoLdKEE4ZLyFTpsdoDv8Ier68137NK0j2H8ibOtIeHU4zq7i1OOY93ZArjPaZjVkGIzJD9FW8Fjt4spp320pRZsR4_rIWF3tGPaWlchBxtxqdmGseBQcJ-m_BI9620s8Oo8L9GP9e3m5q65__bl6831feNaJWjDmVXQMdZLqbyQFGBrmWeUg-bMCei13IrOEcao1VQQ7ZmizHra9kwLpvglenvq3ef0e4JSzRCKgxjtCGkqRkotFVPdHGxPQZdTKRl6s89hsPloKDELb7PANAtMozvzwNvQ-ezNuX_aDuAfj86AZ3998g8hwvG_Os369jNbjEXX3YO6PPTpVAQzrT8BsikuwOjAhwyuGp_Cv3_6F1_qofo</recordid><startdate>19960205</startdate><enddate>19960205</enddate><creator>Van Walraven, Hendrika S.</creator><creator>Strotmann, Heinrich</creator><creator>Schwarz, Oliver</creator><creator>Rumberg, Bernd</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>19960205</creationdate><title>The H +/ATP coupling ratio of the ATP synthase from thiol-modulated chloroplasts and two cyanobacterial strains is four</title><author>Van Walraven, Hendrika S. ; Strotmann, Heinrich ; Schwarz, Oliver ; Rumberg, Bernd</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4861-32a8e522f778d671eeba2d213e932c6ef97b65c0221a91609d2812ad14f296283</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>ATP synthase, H</topic><topic>Chloroplasts</topic><topic>Chloroplasts - metabolism</topic><topic>Cyanobacteria</topic><topic>Cyanobacteria - enzymology</topic><topic>Energy transduction</topic><topic>Enzyme regulation</topic><topic>H +/ATP ratio</topic><topic>hydrophilic part of the ATP synthase (prefix C refers to chloroplasts)</topic><topic>membrane-bound part of the ATP synthase</topic><topic>N-(1-naphtyl)ethylenediamine</topic><topic>NED</topic><topic>phosphate potential</topic><topic>proton electrochemical potential difference</topic><topic>Proton gradient</topic><topic>Proton translocation</topic><topic>Proton-Translocating ATPases - metabolism</topic><topic>standard free energy</topic><topic>Thermodynamics</topic><topic>ΔG p</topic><topic>ΔG ′ 0</topic><topic>Δμ¯H</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Van Walraven, Hendrika S.</creatorcontrib><creatorcontrib>Strotmann, Heinrich</creatorcontrib><creatorcontrib>Schwarz, Oliver</creatorcontrib><creatorcontrib>Rumberg, Bernd</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>Van Walraven, Hendrika S.</au><au>Strotmann, Heinrich</au><au>Schwarz, Oliver</au><au>Rumberg, Bernd</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The H +/ATP coupling ratio of the ATP synthase from thiol-modulated chloroplasts and two cyanobacterial strains is four</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1996-02-05</date><risdate>1996</risdate><volume>379</volume><issue>3</issue><spage>309</spage><epage>313</epage><pages>309-313</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>In this paper the authors emphasise that the proton translocating ATP synthase from thiol-modulated chloroplasts and two cyanobacterial strains has a coupling ratio of 4 protons per ATP synthesised or hydrolysed. This ratio is determined by several thermodynamic studies at equilibrium between phosphate potential (
ΔG
p) and proton gradient (
Δ
μ
H+
), and is confirmed by measurement of proton flux during ATP hydrolysis. Ratios lower than 4 H
+/ATP that have been published in the past have predominantly been determined with the oxidised chloroplast enzyme. Errors in these measurements will be discussed.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>8603713</pmid><doi>10.1016/0014-5793(95)01536-1</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1996-02, Vol.379 (3), p.309-313 |
| issn | 0014-5793 1873-3468 |
| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | ATP synthase, H Chloroplasts Chloroplasts - metabolism Cyanobacteria Cyanobacteria - enzymology Energy transduction Enzyme regulation H +/ATP ratio hydrophilic part of the ATP synthase (prefix C refers to chloroplasts) membrane-bound part of the ATP synthase N-(1-naphtyl)ethylenediamine NED phosphate potential proton electrochemical potential difference Proton gradient Proton translocation Proton-Translocating ATPases - metabolism standard free energy Thermodynamics ΔG p ΔG ′ 0 Δμ¯H |
| title | The H +/ATP coupling ratio of the ATP synthase from thiol-modulated chloroplasts and two cyanobacterial strains is four |
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