| pubmed-article:6831561 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6831561 | lifeskim:mentions | umls-concept:C0038402 | lld:lifeskim |
| pubmed-article:6831561 | lifeskim:mentions | umls-concept:C0022262 | lld:lifeskim |
| pubmed-article:6831561 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:6831561 | lifeskim:mentions | umls-concept:C1948027 | lld:lifeskim |
| pubmed-article:6831561 | lifeskim:mentions | umls-concept:C0440043 | lld:lifeskim |
| pubmed-article:6831561 | lifeskim:mentions | umls-concept:C1705994 | lld:lifeskim |
| pubmed-article:6831561 | lifeskim:mentions | umls-concept:C1513492 | lld:lifeskim |
| pubmed-article:6831561 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:6831561 | pubmed:dateCreated | 1983-5-27 | lld:pubmed |
| pubmed-article:6831561 | pubmed:abstractText | The torque generated by the flagellar motor of Streptococcus strain V4051 has been determined from rates of rotation of cells tethered by a single flagellum in media of different isotopic composition and temperature. Starved cells were energized artificially with either a potassium diffusion potential or a pH gradient. The torque increased linearly with protonmotive force. Identical results were obtained in media made with D2O or H2O; there was no solvent isotope effect. At a fixed protonmotive force, the torque was approximately constant over a temperature range of 4 degrees -38 degrees C. In cells chemotactically inert to changes in cytoplasmic pH, the motor turned counterclockwise when protons moved inward and clockwise when they moved outward. We conclude that the motor is a reversible engine driven by simple acid-base dissociation. A detailed model is discussed. | lld:pubmed |
| pubmed-article:6831561 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6831561 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6831561 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6831561 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6831561 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6831561 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:6831561 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:6831561 | pubmed:author | pubmed-author:BergH CHC | lld:pubmed |
| pubmed-article:6831561 | pubmed:author | pubmed-author:KhanSS | lld:pubmed |
| pubmed-article:6831561 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6831561 | pubmed:volume | 32 | lld:pubmed |
| pubmed-article:6831561 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6831561 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6831561 | pubmed:pagination | 913-9 | lld:pubmed |
| pubmed-article:6831561 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:6831561 | pubmed:year | 1983 | lld:pubmed |
| pubmed-article:6831561 | pubmed:articleTitle | Isotope and thermal effects in chemiosmotic coupling to the flagellar motor of Streptococcus. | lld:pubmed |
| pubmed-article:6831561 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6831561 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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