Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:9683474rdf:typepubmed:Citationlld:pubmed
pubmed-article:9683474lifeskim:mentionsumls-concept:C0995538lld:lifeskim
pubmed-article:9683474lifeskim:mentionsumls-concept:C0080194lld:lifeskim
pubmed-article:9683474lifeskim:mentionsumls-concept:C0013846lld:lifeskim
pubmed-article:9683474lifeskim:mentionsumls-concept:C0007012lld:lifeskim
pubmed-article:9683474lifeskim:mentionsumls-concept:C1280500lld:lifeskim
pubmed-article:9683474lifeskim:mentionsumls-concept:C0033727lld:lifeskim
pubmed-article:9683474lifeskim:mentionsumls-concept:C0243144lld:lifeskim
pubmed-article:9683474lifeskim:mentionsumls-concept:C0443213lld:lifeskim
pubmed-article:9683474lifeskim:mentionsumls-concept:C1314939lld:lifeskim
pubmed-article:9683474pubmed:issue15lld:pubmed
pubmed-article:9683474pubmed:dateCreated1998-8-20lld:pubmed
pubmed-article:9683474pubmed:abstractTextThe product of pxcA (formerly known as cotA) is involved in light-induced Na+-dependent proton extrusion. In the presence of 2, 5-dimethyl-p-benzoquinone, net proton extrusion by Synechocystis sp. strain PCC6803 ceased after 1 min of illumination and a postillumination influx of protons was observed, suggesting that the PxcA-dependent, light-dependent proton extrusion equilibrates with a light-independent influx of protons. A photosystem I (PS I) deletion mutant extruded a large number of protons in the light. Thus, PS II-dependent electron transfer and proton translocation are major factors in light-driven proton extrusion, presumably mediated by ATP synthesis. Inhibition of CO2 fixation by glyceraldehyde in a cytochrome c oxidase (COX) deletion mutant strongly inhibited the proton extrusion. Leakage of PS II-generated electrons to oxygen via COX appears to be required for proton extrusion when CO2 fixation is inhibited. At pH 8.0, NO3- uptake activity was very low in the pxcA mutant at low [Na+] (approximately 100 microM). At pH 6.5, the pxcA strain did not take up CO2 or NO3- at low [Na+] and showed very low CO2 uptake activity even at 15 mM Na+. A possible role of PxcA-dependent proton exchange in charge and pH homeostasis during uptake of CO2, HCO3-, and NO3- is discussed.lld:pubmed
pubmed-article:9683474pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9683474pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9683474pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9683474pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9683474pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9683474pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9683474pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9683474pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9683474pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9683474pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9683474pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9683474pubmed:languageenglld:pubmed
pubmed-article:9683474pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9683474pubmed:citationSubsetIMlld:pubmed
pubmed-article:9683474pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9683474pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9683474pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9683474pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9683474pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9683474pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9683474pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9683474pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9683474pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9683474pubmed:statusMEDLINElld:pubmed
pubmed-article:9683474pubmed:monthAuglld:pubmed
pubmed-article:9683474pubmed:issn0021-9193lld:pubmed
pubmed-article:9683474pubmed:authorpubmed-author:OgawaTTlld:pubmed
pubmed-article:9683474pubmed:authorpubmed-author:SchmettererGGlld:pubmed
pubmed-article:9683474pubmed:authorpubmed-author:SonodaMMlld:pubmed
pubmed-article:9683474pubmed:authorpubmed-author:KatohHHlld:pubmed
pubmed-article:9683474pubmed:authorpubmed-author:VermaasWWlld:pubmed
pubmed-article:9683474pubmed:issnTypePrintlld:pubmed
pubmed-article:9683474pubmed:volume180lld:pubmed
pubmed-article:9683474pubmed:ownerNLMlld:pubmed
pubmed-article:9683474pubmed:authorsCompleteYlld:pubmed
pubmed-article:9683474pubmed:pagination3799-803lld:pubmed
pubmed-article:9683474pubmed:dateRevised2010-9-13lld:pubmed
pubmed-article:9683474pubmed:meshHeadingpubmed-meshheading:9683474-...lld:pubmed
pubmed-article:9683474pubmed:meshHeadingpubmed-meshheading:9683474-...lld:pubmed
pubmed-article:9683474pubmed:meshHeadingpubmed-meshheading:9683474-...lld:pubmed
pubmed-article:9683474pubmed:meshHeadingpubmed-meshheading:9683474-...lld:pubmed
pubmed-article:9683474pubmed:meshHeadingpubmed-meshheading:9683474-...lld:pubmed
pubmed-article:9683474pubmed:meshHeadingpubmed-meshheading:9683474-...lld:pubmed
pubmed-article:9683474pubmed:meshHeadingpubmed-meshheading:9683474-...lld:pubmed
pubmed-article:9683474pubmed:meshHeadingpubmed-meshheading:9683474-...lld:pubmed
pubmed-article:9683474pubmed:meshHeadingpubmed-meshheading:9683474-...lld:pubmed
pubmed-article:9683474pubmed:meshHeadingpubmed-meshheading:9683474-...lld:pubmed
pubmed-article:9683474pubmed:meshHeadingpubmed-meshheading:9683474-...lld:pubmed
pubmed-article:9683474pubmed:meshHeadingpubmed-meshheading:9683474-...lld:pubmed
pubmed-article:9683474pubmed:meshHeadingpubmed-meshheading:9683474-...lld:pubmed
pubmed-article:9683474pubmed:meshHeadingpubmed-meshheading:9683474-...lld:pubmed
pubmed-article:9683474pubmed:meshHeadingpubmed-meshheading:9683474-...lld:pubmed
pubmed-article:9683474pubmed:year1998lld:pubmed
pubmed-article:9683474pubmed:articleTitlePhotosynthetic electron transport involved in PxcA-dependent proton extrusion in Synechocystis sp. Strain PCC6803: effect of pxcA inactivation on CO2, HCO3-, and NO3- uptake.lld:pubmed
pubmed-article:9683474pubmed:affiliationGraduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-01, Japan.lld:pubmed
pubmed-article:9683474pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9683474pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9683474lld:pubmed