| pubmed-article:139610 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:139610 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:139610 | lifeskim:mentions | umls-concept:C1442080 | lld:lifeskim |
| pubmed-article:139610 | lifeskim:mentions | umls-concept:C1948027 | lld:lifeskim |
| pubmed-article:139610 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:139610 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:139610 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:139610 | pubmed:dateCreated | 1977-5-12 | lld:pubmed |
| pubmed-article:139610 | pubmed:abstractText | Purified dicyclohexylcarbodiimide-sensitive ATPase (TF0-F1) from thermophilic bacterium PS3 is composed of a water soluble part with ATP hydrolytic activity (TF1) and a water insoluble moiety (TF0). All of the five subunits (alpha, beta, gamma, delta, and epsilon) of TF1 were isolated. TF1 was reconstituted from the five subunits, which catalyzed an ATP-32Pi exchange and an ATP-driven enhancement of fluorescence of 1-anilinonaphthalene-8-sulfonate, when adsorbed on proteoliposome inlaid with TF0 (TF3-vesicles). Subunit epsilon and/or delta became firmly bound to TF0-vesicles and there was no preferential sequence in the binding. Both subunits were required for binding of the remaining subunits of TF1 to TF0-vesicles, but they did not modify the high H+ -permeability of TF0-vesicles. The addition of gamma but they did not modify the high H+-permeability of TFO-vesicles. The addition of gamma subunit together with epsilon and delta subunits caused a marked decrease of H+ -permeability of TF0-vesicles, similar to that induced by TF1. We conclude tentatively that the epsilon and delta subunits connect TF0 and the other subunits forming a part of a proton pathway, gamma is a gate of proton flow coupled to ATP hydrolysis (or synthesis), and alpha and beta subunits contain the active site for energy transformation. A possible model of subunit structure of TF1 is proposed. | lld:pubmed |
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| pubmed-article:139610 | pubmed:language | eng | lld:pubmed |
| pubmed-article:139610 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:139610 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:139610 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:139610 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:139610 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:139610 | pubmed:author | pubmed-author:YoshidaMM | lld:pubmed |
| pubmed-article:139610 | pubmed:author | pubmed-author:HirataHH | lld:pubmed |
| pubmed-article:139610 | pubmed:author | pubmed-author:KagawaYY | lld:pubmed |
| pubmed-article:139610 | pubmed:author | pubmed-author:SoniJJ | lld:pubmed |
| pubmed-article:139610 | pubmed:author | pubmed-author:OkamotoHH | lld:pubmed |
| pubmed-article:139610 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:139610 | pubmed:volume | 74 | lld:pubmed |
| pubmed-article:139610 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:139610 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:139610 | pubmed:pagination | 936-40 | lld:pubmed |
| pubmed-article:139610 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:139610 | pubmed:year | 1977 | lld:pubmed |
| pubmed-article:139610 | pubmed:articleTitle | Reconstitution of thermostable ATPase capable of energy coupling from its purified subunits. | lld:pubmed |
| pubmed-article:139610 | pubmed:publicationType | Journal Article | lld:pubmed |
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