pubmed-article:11069658 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11069658 | lifeskim:mentions | umls-concept:C0003732 | lld:lifeskim |
pubmed-article:11069658 | lifeskim:mentions | umls-concept:C0524829 | lld:lifeskim |
pubmed-article:11069658 | lifeskim:mentions | umls-concept:C0025516 | lld:lifeskim |
pubmed-article:11069658 | lifeskim:mentions | umls-concept:C0030054 | lld:lifeskim |
pubmed-article:11069658 | lifeskim:mentions | umls-concept:C0038836 | lld:lifeskim |
pubmed-article:11069658 | lifeskim:mentions | umls-concept:C0150543 | lld:lifeskim |
pubmed-article:11069658 | lifeskim:mentions | umls-concept:C0971052 | lld:lifeskim |
pubmed-article:11069658 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:11069658 | pubmed:dateCreated | 2000-12-12 | lld:pubmed |
pubmed-article:11069658 | pubmed:abstractText | Archaeoglobus fulgidus is a hyperthermophilic sulphate-reducing archaeon. It has an optimum growth temperature of 83 degrees C and is described as a strict anaerobe. Its genome lacks any homologue of canonical superoxide (O2.-) dismutases. In this work, we show that neelaredoxin (Nlr) is the main O2.- scavenger in A. fulgidus, by studying both the wild-type and recombinant proteins. Nlr is a 125-amino-acid blue-coloured protein containing a single iron atom/molecule, which in the oxidized state is high spin ferric. This iron centre has a reduction potential of +230 mV at pH 7.0. Nitroblue tetrazolium-stained gel assays of cell-soluble extracts show that Nlr is the main protein from A. fulgidus which is reactive towards O2.-. Furthermore, it is shown that Nlr is able to both reduce and dismutate O2.-, thus having a bifunctional reactivity towards O2.-. Kinetic and spectroscopic studies indicate that Nlr's superoxide reductase activity may allow the cell to eliminate O2.- quickly in a NAD(P)H-dependent pathway. On the other hand, Nlr's superoxide dismutation activity will allow the cell to detoxify O2.- independently of the cell redox status. Its superoxide dismutase activity was estimated to be 59 U mg-1 by the xanthine/xanthine oxidase assay at 25 degrees C. Pulse radiolysis studies with the isolated and reduced Nlr proved unambiguously that it has superoxide dismutase activity; at pH 7.1 and 83 degrees C, the rate constant is 5 x 106 M-1 s-1. Besides the superoxide dismutase activity, soluble cell extracts of A. fulgidus also exhibit catalase and NAD(P)H/oxygen oxidoreductase activities. By putting these findings together with the entire genomic data available, a possible oxygen detoxification mechanism in A. fulgidus is discussed. | lld:pubmed |
pubmed-article:11069658 | pubmed:language | eng | lld:pubmed |
pubmed-article:11069658 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11069658 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11069658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11069658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11069658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11069658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11069658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11069658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11069658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11069658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11069658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11069658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11069658 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11069658 | pubmed:month | Oct | lld:pubmed |
pubmed-article:11069658 | pubmed:issn | 0950-382X | lld:pubmed |
pubmed-article:11069658 | pubmed:author | pubmed-author:HuberHH | lld:pubmed |
pubmed-article:11069658 | pubmed:author | pubmed-author:StetterK OKO | lld:pubmed |
pubmed-article:11069658 | pubmed:author | pubmed-author:TeixeiraMM | lld:pubmed |
pubmed-article:11069658 | pubmed:author | pubmed-author:CabelloBB | lld:pubmed |
pubmed-article:11069658 | pubmed:author | pubmed-author:SaraivaL MLM | lld:pubmed |
pubmed-article:11069658 | pubmed:author | pubmed-author:AbreuI AIA | lld:pubmed |
pubmed-article:11069658 | pubmed:author | pubmed-author:CaritaJJ | lld:pubmed |
pubmed-article:11069658 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11069658 | pubmed:volume | 38 | lld:pubmed |
pubmed-article:11069658 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11069658 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11069658 | pubmed:pagination | 322-34 | lld:pubmed |
pubmed-article:11069658 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:11069658 | pubmed:year | 2000 | lld:pubmed |
pubmed-article:11069658 | pubmed:articleTitle | Oxygen detoxification in the strict anaerobic archaeon Archaeoglobus fulgidus: superoxide scavenging by neelaredoxin. | lld:pubmed |
pubmed-article:11069658 | pubmed:affiliation | Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, 2780-156 Oeiras, Portugal. | lld:pubmed |
pubmed-article:11069658 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11069658 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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