| pubmed-article:16014708 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16014708 | lifeskim:mentions | umls-concept:C0043047 | lld:lifeskim |
| pubmed-article:16014708 | lifeskim:mentions | umls-concept:C0010760 | lld:lifeskim |
| pubmed-article:16014708 | lifeskim:mentions | umls-concept:C0597391 | lld:lifeskim |
| pubmed-article:16014708 | lifeskim:mentions | umls-concept:C0033727 | lld:lifeskim |
| pubmed-article:16014708 | lifeskim:mentions | umls-concept:C1547239 | lld:lifeskim |
| pubmed-article:16014708 | pubmed:issue | 30 | lld:pubmed |
| pubmed-article:16014708 | pubmed:dateCreated | 2005-7-27 | lld:pubmed |
| pubmed-article:16014708 | pubmed:abstractText | The membrane-bound enzyme cytochrome c oxidase is responsible for cell respiration in aerobic organisms and conserves free energy from O2 reduction into an electrochemical proton gradient by coupling the redox reaction to proton-pumping across the membrane. O2 reduction produces water at the bimetallic heme a3/CuB active site next to a hydrophobic cavity deep within the membrane. Water molecules in this cavity have been suggested to play an important role in the proton-pumping mechanism. Here, we show by molecular dynamics simulations that the conserved arginine/heme a3 delta-propionate ion pair provides a gate, which exhibits reversible thermal opening that is governed by the redox state and the water molecules in the cavity. An important role of this gate in the proton-pumping mechanism is supported by site-directed mutagenesis experiments. Transport of the product water out of the enzyme must be rigidly controlled to prevent water-mediated proton leaks that could compromise the proton-pumping function. Exit of product water is observed through the same arginine/propionate gate, which provides an explanation for the observed extraordinary spatial specificity of water expulsion from the enzyme. | lld:pubmed |
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| pubmed-article:16014708 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16014708 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16014708 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16014708 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16014708 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:16014708 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:16014708 | pubmed:author | pubmed-author:PuustinenAnne... | lld:pubmed |
| pubmed-article:16014708 | pubmed:author | pubmed-author:WikströmMårte... | lld:pubmed |
| pubmed-article:16014708 | pubmed:author | pubmed-author:LaakkonenLiis... | lld:pubmed |
| pubmed-article:16014708 | pubmed:author | pubmed-author:RibackaCamill... | lld:pubmed |
| pubmed-article:16014708 | pubmed:author | pubmed-author:MolinMikaM | lld:pubmed |
| pubmed-article:16014708 | pubmed:author | pubmed-author:VerkhovskyMic... | lld:pubmed |
| pubmed-article:16014708 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16014708 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:16014708 | pubmed:volume | 102 | lld:pubmed |
| pubmed-article:16014708 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16014708 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16014708 | pubmed:pagination | 10478-81 | lld:pubmed |
| pubmed-article:16014708 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:16014708 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16014708 | pubmed:articleTitle | Gating of proton and water transfer in the respiratory enzyme cytochrome c oxidase. | lld:pubmed |
| pubmed-article:16014708 | pubmed:affiliation | Helsinki Bioenergetics Group, Institute of Biotechnology, Program for Structural Biology and Biophysics, University of Helsinki, PB 65 (Viikinkaari 1), 00014 Helsinki, Finland. marten.wikstrom@helsinki.fi | lld:pubmed |
| pubmed-article:16014708 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16014708 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:16014708 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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