| pubmed-article:10811225 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10811225 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:10811225 | lifeskim:mentions | umls-concept:C0521119 | lld:lifeskim |
| pubmed-article:10811225 | lifeskim:mentions | umls-concept:C0013846 | lld:lifeskim |
| pubmed-article:10811225 | lifeskim:mentions | umls-concept:C0034435 | lld:lifeskim |
| pubmed-article:10811225 | pubmed:issue | 6782 | lld:pubmed |
| pubmed-article:10811225 | pubmed:dateCreated | 2000-5-23 | lld:pubmed |
| pubmed-article:10811225 | pubmed:abstractText | Respiratory processes in bacteria are remarkable because of their ability to use a variety of compounds, including insoluble minerals, as terminal electron acceptors. Although much is known about microbial electron transport to soluble electron acceptors, little is understood about electron transport to insoluble compounds such as ferric oxides. In anaerobic environments, humic substances can serve as electron acceptors and also as electron shuttles to ferric oxides. To explore this process, we identified mutants in Shewanella putrefaciens that are unable to respire on humic substances. Here we show that these mutants contain disruptions in a gene that is involved in the biosynthesis of menaquinone. During growth, the wild type releases a menaquinone-related redox-active small molecule into the medium that complements the mutants. This finding raises the possibility that electron transfer to a variety of oxidants, including poorly soluble minerals, may be mediated by microbially excreted quinones that have yet to be identified. | lld:pubmed |
| pubmed-article:10811225 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10811225 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10811225 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10811225 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10811225 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10811225 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10811225 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10811225 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10811225 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10811225 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10811225 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10811225 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10811225 | pubmed:month | May | lld:pubmed |
| pubmed-article:10811225 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:10811225 | pubmed:author | pubmed-author:KolterRR | lld:pubmed |
| pubmed-article:10811225 | pubmed:author | pubmed-author:NewmanD KDK | lld:pubmed |
| pubmed-article:10811225 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10811225 | pubmed:day | 4 | lld:pubmed |
| pubmed-article:10811225 | pubmed:volume | 405 | lld:pubmed |
| pubmed-article:10811225 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10811225 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10811225 | pubmed:pagination | 94-7 | lld:pubmed |
| pubmed-article:10811225 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:10811225 | pubmed:meshHeading | pubmed-meshheading:10811225... | lld:pubmed |
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| pubmed-article:10811225 | pubmed:meshHeading | pubmed-meshheading:10811225... | lld:pubmed |
| pubmed-article:10811225 | pubmed:meshHeading | pubmed-meshheading:10811225... | lld:pubmed |
| pubmed-article:10811225 | pubmed:meshHeading | pubmed-meshheading:10811225... | lld:pubmed |
| pubmed-article:10811225 | pubmed:meshHeading | pubmed-meshheading:10811225... | lld:pubmed |
| pubmed-article:10811225 | pubmed:meshHeading | pubmed-meshheading:10811225... | lld:pubmed |
| pubmed-article:10811225 | pubmed:meshHeading | pubmed-meshheading:10811225... | lld:pubmed |
| pubmed-article:10811225 | pubmed:meshHeading | pubmed-meshheading:10811225... | lld:pubmed |
| pubmed-article:10811225 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10811225 | pubmed:articleTitle | A role for excreted quinones in extracellular electron transfer. | lld:pubmed |
| pubmed-article:10811225 | pubmed:affiliation | Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA. dkn@gps.caltech.edu | lld:pubmed |
| pubmed-article:10811225 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10811225 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10811225 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:10811225 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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