| pubmed-article:18439144 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18439144 | lifeskim:mentions | umls-concept:C2752508 | lld:lifeskim |
| pubmed-article:18439144 | lifeskim:mentions | umls-concept:C0441635 | lld:lifeskim |
| pubmed-article:18439144 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:18439144 | lifeskim:mentions | umls-concept:C1167322 | lld:lifeskim |
| pubmed-article:18439144 | lifeskim:mentions | umls-concept:C0010749 | lld:lifeskim |
| pubmed-article:18439144 | lifeskim:mentions | umls-concept:C0030016 | lld:lifeskim |
| pubmed-article:18439144 | lifeskim:mentions | umls-concept:C0205419 | lld:lifeskim |
| pubmed-article:18439144 | lifeskim:mentions | umls-concept:C0020306 | lld:lifeskim |
| pubmed-article:18439144 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:18439144 | lifeskim:mentions | umls-concept:C0018966 | lld:lifeskim |
| pubmed-article:18439144 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:18439144 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:18439144 | pubmed:dateCreated | 2008-7-24 | lld:pubmed |
| pubmed-article:18439144 | pubmed:abstractText | Members of the NapC/NrfH family are multihaem c-type cytochromes that exchange electrons with oxidoreductases situated at the outside of the cytoplasmic membrane or in the periplasmic space of many proteobacteria. They form a group of membrane-bound quinol dehydrogenases that are essential components of several electron transport chains, for example those of periplasmic nitrate respiration and respiratory nitrite ammonification. Knowledge of the structure-function relationships of NapC/NrfH proteins is scarce and only one high-resolution structure (Desulfovibrio vulgaris NrfH) is available. In the present study, several Wolinella succinogenes mutants that produce variants of NrfH, the membrane anchor of the cytochrome c nitrite reductase complex, were constructed and characterized in order to improve the understanding of the putative menaquinol-binding site, the maturation and function of the four covalently bound haem c groups and the importance of the N-terminal transmembrane segment. Based on amino acid sequence alignments, a homology model for W. succinogenes NrfH was constructed that underlines the overall conservation of tertiary structure in spite of a low sequence homology. The results support the proposed architecture of the menaquinol-binding site in D. vulgaris NrfH, demonstrate that each histidine residue arranged in one of the four CX(2)CH haem c-binding motifs is essential for NrfH maturation in W. succinogenes, and indicate a limited flexibility towards the length and structure of the transmembrane region. | lld:pubmed |
| pubmed-article:18439144 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18439144 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18439144 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18439144 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18439144 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18439144 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18439144 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18439144 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18439144 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18439144 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18439144 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18439144 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18439144 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18439144 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18439144 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:18439144 | pubmed:issn | 1470-8728 | lld:pubmed |
| pubmed-article:18439144 | pubmed:author | pubmed-author:EinsleOliverO | lld:pubmed |
| pubmed-article:18439144 | pubmed:author | pubmed-author:SimonJörgJ | lld:pubmed |
| pubmed-article:18439144 | pubmed:author | pubmed-author:KernMelanieM | lld:pubmed |
| pubmed-article:18439144 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18439144 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:18439144 | pubmed:volume | 414 | lld:pubmed |
| pubmed-article:18439144 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18439144 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18439144 | pubmed:pagination | 73-9 | lld:pubmed |
| pubmed-article:18439144 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:18439144 | pubmed:meshHeading | pubmed-meshheading:18439144... | lld:pubmed |
| pubmed-article:18439144 | pubmed:meshHeading | pubmed-meshheading:18439144... | lld:pubmed |
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| pubmed-article:18439144 | pubmed:meshHeading | pubmed-meshheading:18439144... | lld:pubmed |
| pubmed-article:18439144 | pubmed:meshHeading | pubmed-meshheading:18439144... | lld:pubmed |
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| pubmed-article:18439144 | pubmed:meshHeading | pubmed-meshheading:18439144... | lld:pubmed |
| pubmed-article:18439144 | pubmed:meshHeading | pubmed-meshheading:18439144... | lld:pubmed |
| pubmed-article:18439144 | pubmed:meshHeading | pubmed-meshheading:18439144... | lld:pubmed |
| pubmed-article:18439144 | pubmed:meshHeading | pubmed-meshheading:18439144... | lld:pubmed |
| pubmed-article:18439144 | pubmed:meshHeading | pubmed-meshheading:18439144... | lld:pubmed |
| pubmed-article:18439144 | pubmed:meshHeading | pubmed-meshheading:18439144... | lld:pubmed |
| pubmed-article:18439144 | pubmed:meshHeading | pubmed-meshheading:18439144... | lld:pubmed |
| pubmed-article:18439144 | pubmed:meshHeading | pubmed-meshheading:18439144... | lld:pubmed |
| pubmed-article:18439144 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18439144 | pubmed:articleTitle | Variants of the tetrahaem cytochrome c quinol dehydrogenase NrfH characterize the menaquinol-binding site, the haem c-binding motifs and the transmembrane segment. | lld:pubmed |
| pubmed-article:18439144 | pubmed:affiliation | Institut für Molekulare Biowissenschaften, Johann Wolfgang Goethe-Universität, Max-von-Laue-Str. 9, D-60438 Frankfurt am Main, Germany. | lld:pubmed |
| pubmed-article:18439144 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18439144 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:18439144 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
