| pubmed-article:16629658 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16629658 | lifeskim:mentions | umls-concept:C1257890 | lld:lifeskim |
| pubmed-article:16629658 | lifeskim:mentions | umls-concept:C0023690 | lld:lifeskim |
| pubmed-article:16629658 | lifeskim:mentions | umls-concept:C0003601 | lld:lifeskim |
| pubmed-article:16629658 | lifeskim:mentions | umls-concept:C0010798 | lld:lifeskim |
| pubmed-article:16629658 | lifeskim:mentions | umls-concept:C1254042 | lld:lifeskim |
| pubmed-article:16629658 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:16629658 | pubmed:dateCreated | 2006-4-24 | lld:pubmed |
| pubmed-article:16629658 | pubmed:abstractText | In all organisms, haem is post-translationally and covalently attached to c apocytochromes to produce c holocytochromes via a process called c-type cytochromes maturation, which involves numerous components. In bacteria it was not clear which of these components catalyses the extracytoplasmic haem-apocytochrome ligation per se. In this issue of Molecular Microbiology, Feissner and colleagues report that a single polypeptide from Helicobacter pylori, corresponding to the fusion of two proteins found in other organisms, performs haem ligation to a coexpressed Bordetella pertussis apocytochrome c in an Escherichia coli mutant lacking its own cytochrome c maturation proteins. This simple experimental system pinpoints the components catalysing extracytoplasmic covalent haem ligation and raises intriguing issues about the requirements for delivery of haem and apocytochrome c substrates to produce c holocytochromes. | lld:pubmed |
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| pubmed-article:16629658 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16629658 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16629658 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16629658 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16629658 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16629658 | pubmed:month | May | lld:pubmed |
| pubmed-article:16629658 | pubmed:issn | 0950-382X | lld:pubmed |
| pubmed-article:16629658 | pubmed:author | pubmed-author:DaldalFevziF | lld:pubmed |
| pubmed-article:16629658 | pubmed:author | pubmed-author:SandersCarste... | lld:pubmed |
| pubmed-article:16629658 | pubmed:author | pubmed-author:TurkarslanSer... | lld:pubmed |
| pubmed-article:16629658 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16629658 | pubmed:volume | 60 | lld:pubmed |
| pubmed-article:16629658 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16629658 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16629658 | pubmed:pagination | 537-41 | lld:pubmed |
| pubmed-article:16629658 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:16629658 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16629658 | pubmed:articleTitle | Extracytoplasmic prosthetic group ligation to apoproteins: maturation of c-type cytochromes. | lld:pubmed |
| pubmed-article:16629658 | pubmed:affiliation | University of Pennsylvania, Department of Biology, Plant Science Institute, Philadelphia, PA 19104, USA. | lld:pubmed |
| pubmed-article:16629658 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16629658 | pubmed:publicationType | Comment | lld:pubmed |
| pubmed-article:16629658 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:16629658 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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