| pubmed-article:10727244 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10727244 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:10727244 | lifeskim:mentions | umls-concept:C0001480 | lld:lifeskim |
| pubmed-article:10727244 | lifeskim:mentions | umls-concept:C0001721 | lld:lifeskim |
| pubmed-article:10727244 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:10727244 | lifeskim:mentions | umls-concept:C1511997 | lld:lifeskim |
| pubmed-article:10727244 | lifeskim:mentions | umls-concept:C1705241 | lld:lifeskim |
| pubmed-article:10727244 | lifeskim:mentions | umls-concept:C0439097 | lld:lifeskim |
| pubmed-article:10727244 | lifeskim:mentions | umls-concept:C1547348 | lld:lifeskim |
| pubmed-article:10727244 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:10727244 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:10727244 | pubmed:dateCreated | 2000-5-4 | lld:pubmed |
| pubmed-article:10727244 | pubmed:abstractText | The ATP synthase of Escherichia coli is believed to act through a rotational mechanism in which the b(2)delta subcomplex holds the alphabeta hexamer stationary relative to the rotating gamma and epsilon subunits. We have engineered a disulfide bond between cysteines introduced at position 158 of the delta subunit and at a position just beyond the normal C-terminus of the b subunit. The formation of this disulfide bond verifies that the C-terminal region of b is proximal to residue 158 of delta. The disulfide bond does not affect the ability of the F(1)F(0) complex to hydrolyze ATP, couple ATP hydrolysis to the establishment of a proton gradient, or maintain a proton gradient generated by the electron transport chain. These results are consistent with a permanent association of b(2) with delta as suggested by the rotational model of enzyme function. | lld:pubmed |
| pubmed-article:10727244 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10727244 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10727244 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10727244 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10727244 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10727244 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10727244 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10727244 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10727244 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10727244 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10727244 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10727244 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10727244 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10727244 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:10727244 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:10727244 | pubmed:author | pubmed-author:DunnS DSD | lld:pubmed |
| pubmed-article:10727244 | pubmed:author | pubmed-author:McLachlinD... | lld:pubmed |
| pubmed-article:10727244 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10727244 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:10727244 | pubmed:volume | 39 | lld:pubmed |
| pubmed-article:10727244 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10727244 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10727244 | pubmed:pagination | 3486-90 | lld:pubmed |
| pubmed-article:10727244 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:10727244 | pubmed:meshHeading | pubmed-meshheading:10727244... | lld:pubmed |
| pubmed-article:10727244 | pubmed:meshHeading | pubmed-meshheading:10727244... | lld:pubmed |
| pubmed-article:10727244 | pubmed:meshHeading | pubmed-meshheading:10727244... | lld:pubmed |
| pubmed-article:10727244 | pubmed:meshHeading | pubmed-meshheading:10727244... | lld:pubmed |
| pubmed-article:10727244 | pubmed:meshHeading | pubmed-meshheading:10727244... | lld:pubmed |
| pubmed-article:10727244 | pubmed:meshHeading | pubmed-meshheading:10727244... | lld:pubmed |
| pubmed-article:10727244 | pubmed:meshHeading | pubmed-meshheading:10727244... | lld:pubmed |
| pubmed-article:10727244 | pubmed:meshHeading | pubmed-meshheading:10727244... | lld:pubmed |
| pubmed-article:10727244 | pubmed:meshHeading | pubmed-meshheading:10727244... | lld:pubmed |
| pubmed-article:10727244 | pubmed:meshHeading | pubmed-meshheading:10727244... | lld:pubmed |
| pubmed-article:10727244 | pubmed:meshHeading | pubmed-meshheading:10727244... | lld:pubmed |
| pubmed-article:10727244 | pubmed:meshHeading | pubmed-meshheading:10727244... | lld:pubmed |
| pubmed-article:10727244 | pubmed:meshHeading | pubmed-meshheading:10727244... | lld:pubmed |
| pubmed-article:10727244 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10727244 | pubmed:articleTitle | Disulfide linkage of the b and delta subunits does not affect the function of the Escherichia coli ATP synthase. | lld:pubmed |
| pubmed-article:10727244 | pubmed:affiliation | Department of Biochemistry, University of Western Ontario, London, Ontario, Canada N6A 5C1. | lld:pubmed |
| pubmed-article:10727244 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10727244 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:948247 | entrezgene:pubmed | pubmed-article:10727244 | lld:entrezgene |
| entrez-gene:948243 | entrezgene:pubmed | pubmed-article:10727244 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10727244 | lld:pubmed |
