| pubmed-article:18536726 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18536726 | lifeskim:mentions | umls-concept:C0035203 | lld:lifeskim |
| pubmed-article:18536726 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:18536726 | lifeskim:mentions | umls-concept:C1621943 | lld:lifeskim |
| pubmed-article:18536726 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:18536726 | lifeskim:mentions | umls-concept:C0071687 | lld:lifeskim |
| pubmed-article:18536726 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:18536726 | pubmed:dateCreated | 2008-7-3 | lld:pubmed |
| pubmed-article:18536726 | pubmed:abstractText | Bacterial polysulfide reductase (PsrABC) is an integral membrane protein complex responsible for quinone-coupled reduction of polysulfide, a process important in extreme environments such as deep-sea vents and hot springs. We determined the structure of polysulfide reductase from Thermus thermophilus at 2.4-A resolution, revealing how the PsrA subunit recognizes and reduces its unique polyanionic substrate. The integral membrane subunit PsrC was characterized using the natural substrate menaquinone-7 and inhibitors, providing a comprehensive representation of a quinone binding site and revealing the presence of a water-filled cavity connecting the quinone binding site on the periplasmic side to the cytoplasm. These results suggest that polysulfide reductase could be a key energy-conserving enzyme of the T. thermophilus respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane via a previously unknown mechanism. | lld:pubmed |
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| pubmed-article:18536726 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18536726 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18536726 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18536726 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18536726 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:18536726 | pubmed:issn | 1545-9985 | lld:pubmed |
| pubmed-article:18536726 | pubmed:author | pubmed-author:YanoTakahiroT | lld:pubmed |
| pubmed-article:18536726 | pubmed:author | pubmed-author:JormakkaMikaM | lld:pubmed |
| pubmed-article:18536726 | pubmed:author | pubmed-author:IwataSoS | lld:pubmed |
| pubmed-article:18536726 | pubmed:author | pubmed-author:YokoyamaKenK | lld:pubmed |
| pubmed-article:18536726 | pubmed:author | pubmed-author:TamakoshiMasa... | lld:pubmed |
| pubmed-article:18536726 | pubmed:author | pubmed-author:ShimamuraTats... | lld:pubmed |
| pubmed-article:18536726 | pubmed:author | pubmed-author:AkimotoSatoru... | lld:pubmed |
| pubmed-article:18536726 | pubmed:author | pubmed-author:CurmiPaulP | lld:pubmed |
| pubmed-article:18536726 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18536726 | pubmed:volume | 15 | lld:pubmed |
| pubmed-article:18536726 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18536726 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18536726 | pubmed:pagination | 730-7 | lld:pubmed |
| pubmed-article:18536726 | pubmed:dateRevised | 2010-9-21 | lld:pubmed |
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