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| pubmed-article:11525168 | lifeskim:mentions | umls-concept:C0524829 | lld:lifeskim |
| pubmed-article:11525168 | lifeskim:mentions | umls-concept:C0027303 | lld:lifeskim |
| pubmed-article:11525168 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:11525168 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:11525168 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:11525168 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:11525168 | lifeskim:mentions | umls-concept:C0243839 | lld:lifeskim |
| pubmed-article:11525168 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:11525168 | pubmed:dateCreated | 2001-8-29 | lld:pubmed |
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| pubmed-article:11525168 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11525168 | pubmed:abstractText | Studies performed within the last decade have indicated that microbial reduction of Fe(III) to Fe(II) is a biologically significant process. The ferric reductase (FeR) from Archaeoglobus fulgidus is the first reported archaeal ferric reductase and it catalyzes the flavin-mediated reduction of ferric iron complexes using NAD(P)H as the electron donor. Based on its catalytic activity, the A. fulgidus FeR resembles the bacterial and eukaryotic assimilatory type of ferric reductases. However, the high cellular abundance of the A. fulgidus FeR (approximately 0.75% of the total soluble protein) suggests a catabolic role for this enzyme as the terminal electron acceptor in a ferric iron-based respiratory pathway [1]. | lld:pubmed |
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| pubmed-article:11525168 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11525168 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11525168 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11525168 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:11525168 | pubmed:issn | 0969-2126 | lld:pubmed |
| pubmed-article:11525168 | pubmed:author | pubmed-author:JohnsonEE | lld:pubmed |
| pubmed-article:11525168 | pubmed:author | pubmed-author:ReesD CDC | lld:pubmed |
| pubmed-article:11525168 | pubmed:author | pubmed-author:SchröderII | lld:pubmed |
| pubmed-article:11525168 | pubmed:author | pubmed-author:ChiuH JHJ | lld:pubmed |
| pubmed-article:11525168 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11525168 | pubmed:day | 4 | lld:pubmed |
| pubmed-article:11525168 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:11525168 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11525168 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11525168 | pubmed:pagination | 311-9 | lld:pubmed |
| pubmed-article:11525168 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:11525168 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11525168 | pubmed:articleTitle | Crystal structures of a novel ferric reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus and its complex with NADP+. | lld:pubmed |
| pubmed-article:11525168 | pubmed:affiliation | Division of Chemistry and Chemical Engineering, California Institute of Technology, 91125, USA. | lld:pubmed |
| pubmed-article:11525168 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11525168 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11525168 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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