| pubmed-article:1715764 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1715764 | lifeskim:mentions | umls-concept:C0026336 | lld:lifeskim |
| pubmed-article:1715764 | lifeskim:mentions | umls-concept:C0043047 | lld:lifeskim |
| pubmed-article:1715764 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:1715764 | lifeskim:mentions | umls-concept:C0018165 | lld:lifeskim |
| pubmed-article:1715764 | lifeskim:mentions | umls-concept:C0033727 | lld:lifeskim |
| pubmed-article:1715764 | lifeskim:mentions | umls-concept:C0005978 | lld:lifeskim |
| pubmed-article:1715764 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:1715764 | pubmed:dateCreated | 1991-10-9 | lld:pubmed |
| pubmed-article:1715764 | pubmed:abstractText | The gramicidin channel contains a single strand of water molecules associated through hydrogen bonds. Previous work has shown that channels of similar size are formed by association of transmembrane alpha helices of synthetic leucine-serine peptides. Both types of channels translocate protons with considerable selectivity relative to other cations, and it has been proposed that the selectivity arises by proton "hopping" along hydrogen-bonded chains of water, whereas other cations must cross by ordinary diffusion processes. It is possible that a similar mechanism underlies proton transport in the Fo subunit of the F1F0 ATP synthase. Using the gramicidin channel as a model, we have tested whether a single strand of water is kinetically competent to translocate protons at a rate sufficient to support known rates of ATP synthesis. We found that the gramicidin channel saturates at approximately 530 pS of protonic current in 4 M HCl, more than sufficient for typical ATP synthesis rates. It follows that proton diffusion to a putative channel in Fo, rather than the channel itself, may limit ATP synthesis rates. | lld:pubmed |
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| pubmed-article:1715764 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1715764 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1715764 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1715764 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1715764 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:1715764 | pubmed:issn | 0006-3495 | lld:pubmed |
| pubmed-article:1715764 | pubmed:author | pubmed-author:DeamerD WDW | lld:pubmed |
| pubmed-article:1715764 | pubmed:author | pubmed-author:AkesonMM | lld:pubmed |
| pubmed-article:1715764 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1715764 | pubmed:volume | 60 | lld:pubmed |
| pubmed-article:1715764 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1715764 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1715764 | pubmed:pagination | 101-9 | lld:pubmed |
| pubmed-article:1715764 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:1715764 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1715764 | pubmed:articleTitle | Proton conductance by the gramicidin water wire. Model for proton conductance in the F1F0 ATPases? | lld:pubmed |
| pubmed-article:1715764 | pubmed:affiliation | Department of Zoology, University of California, Davis 95616. | lld:pubmed |
| pubmed-article:1715764 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1715764 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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