| pubmed-article:2540148 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2540148 | lifeskim:mentions | umls-concept:C0995884 | lld:lifeskim |
| pubmed-article:2540148 | lifeskim:mentions | umls-concept:C0015858 | lld:lifeskim |
| pubmed-article:2540148 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:2540148 | lifeskim:mentions | umls-concept:C0204727 | lld:lifeskim |
| pubmed-article:2540148 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
| pubmed-article:2540148 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:2540148 | lifeskim:mentions | umls-concept:C0205460 | lld:lifeskim |
| pubmed-article:2540148 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:2540148 | pubmed:dateCreated | 1989-6-7 | lld:pubmed |
| pubmed-article:2540148 | pubmed:abstractText | A ferredoxin has been isolated from the thermophilic methanogen Methanococcus thermolithotrophicus. The native protein was a monomer exhibiting a molecular weight of 7,262, calculated from the amino acid composition. Its absorption spectrum had two maxima at 390 and 283 nm, with an absorbance ratio A390/A283 of 0.79. The absorption at 390 nm (E = 29 mM-1 cm-1) and the content of iron of the protein are in agreement with the presence of two 4Fe-4S clusters in M. thermolithotrophicus ferredoxin. Its amino acid composition showed the presence of eight cysteine residues, which is the required number of cysteines for the binding of two 4Fe-4S clusters. The protein was characterized by the lack of histidine, arginine, and leucine and a high content of valine. It was unusually stable to high temperatures but not to oxygen. The ESR spectrum of the protein in the oxidized state showed a minor signal at g = 2.01, corresponding to an oxidized 3Fe-4S cluster. The protein, which was difficult to reduce with dithionite or reduced mediators, exhibited in its reduced state a spectrum typical of two interacting reduced 4Fe-4S clusters. M. thermolithotrophicus ferredoxin functioned as an electron acceptor for the CO dehydrogenase complex with an extract free of ferredoxin. No reaction was detected with F420 or hydrogenase. | lld:pubmed |
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| pubmed-article:2540148 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2540148 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2540148 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2540148 | pubmed:month | May | lld:pubmed |
| pubmed-article:2540148 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:2540148 | pubmed:author | pubmed-author:BelaichJ PJP | lld:pubmed |
| pubmed-article:2540148 | pubmed:author | pubmed-author:BruschiMM | lld:pubmed |
| pubmed-article:2540148 | pubmed:author | pubmed-author:ChapmanAA | lld:pubmed |
| pubmed-article:2540148 | pubmed:author | pubmed-author:CammackRR | lld:pubmed |
| pubmed-article:2540148 | pubmed:author | pubmed-author:HatchikianE... | lld:pubmed |
| pubmed-article:2540148 | pubmed:author | pubmed-author:FardeauM LML | lld:pubmed |
| pubmed-article:2540148 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2540148 | pubmed:volume | 171 | lld:pubmed |
| pubmed-article:2540148 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2540148 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2540148 | pubmed:pagination | 2384-90 | lld:pubmed |
| pubmed-article:2540148 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2540148 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2540148 | pubmed:articleTitle | Isolation, characterization, and biological activity of the Methanococcus thermolithotrophicus ferredoxin. | lld:pubmed |
| pubmed-article:2540148 | pubmed:affiliation | Laboratoire de Chimie Bactérienne, Centre National de la Recherche Scientifique, Marseille, France. | lld:pubmed |
| pubmed-article:2540148 | pubmed:publicationType | Journal Article | lld:pubmed |
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