| pubmed-article:12755703 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12755703 | lifeskim:mentions | umls-concept:C1057281 | lld:lifeskim |
| pubmed-article:12755703 | lifeskim:mentions | umls-concept:C0016570 | lld:lifeskim |
| pubmed-article:12755703 | lifeskim:mentions | umls-concept:C0030011 | lld:lifeskim |
| pubmed-article:12755703 | lifeskim:mentions | umls-concept:C0392214 | lld:lifeskim |
| pubmed-article:12755703 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:12755703 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:12755703 | pubmed:dateCreated | 2003-5-20 | lld:pubmed |
| pubmed-article:12755703 | pubmed:abstractText | Two formate dehydrogenases (CO2-reductases) (FDH-1 and FDH-2) were isolated from the syntrophic propionate-oxidizing bacterium Syntrophobacter fumaroxidans. Both enzymes were produced in axenic fumarate-grown cells as well as in cells which were grown syntrophically on propionate with Methanospirillum hungatei as the H2 and formate scavenger. The purified enzymes exhibited extremely high formate-oxidation and CO2-reduction rates, and low Km values for formate. For the enzyme designated FDH-1, a specific formate oxidation rate of 700 U.mg-1 and a Km for formate of 0.04 mm were measured when benzyl viologen was used as an artificial electron acceptor. The enzyme designated FDH-2 oxidized formate with a specific activity of 2700 U.mg-1 and a Km of 0.01 mm for formate with benzyl viologen as electron acceptor. The specific CO2-reduction (to formate) rates measured for FDH-1 and FDH-2, using dithionite-reduced methyl viologen as the electron donor, were 900 U.mg-1 and 89 U.mg-1, respectively. From gel filtration and polyacrylamide gel electrophoresis it was concluded that FDH-1 is composed of three subunits (89 +/- 3, 56 +/- 2 and 19 +/- 1 kDa) and has a native molecular mass of approximately 350 kDa. FDH-2 appeared to be a heterodimer composed of a 92 +/- 3 kDa and a 33 +/- 2 kDa subunit. Both enzymes contained tungsten and selenium, while molybdenum was not detected. EPR spectroscopy suggested that FDH-1 contains at least four [2Fe-2S] clusters per molecule and additionally paramagnetically coupled [4Fe-4S] clusters. FDH-2 contains at least two [4Fe-4S] clusters per molecule. As both enzymes are produced under all growth conditions tested, but with differences in levels, expression may depend on unknown parameters. | lld:pubmed |
| pubmed-article:12755703 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12755703 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12755703 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12755703 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12755703 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12755703 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12755703 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12755703 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12755703 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12755703 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12755703 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12755703 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12755703 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:12755703 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:12755703 | pubmed:author | pubmed-author:HagedoornPete... | lld:pubmed |
| pubmed-article:12755703 | pubmed:author | pubmed-author:StamsAlfons... | lld:pubmed |
| pubmed-article:12755703 | pubmed:author | pubmed-author:HagenWilfred... | lld:pubmed |
| pubmed-article:12755703 | pubmed:author | pubmed-author:de BokFrank... | lld:pubmed |
| pubmed-article:12755703 | pubmed:author | pubmed-author:SchiltzEmileE | lld:pubmed |
| pubmed-article:12755703 | pubmed:author | pubmed-author:SilvaPedro... | lld:pubmed |
| pubmed-article:12755703 | pubmed:author | pubmed-author:FritscheKathr... | lld:pubmed |
| pubmed-article:12755703 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12755703 | pubmed:volume | 270 | lld:pubmed |
| pubmed-article:12755703 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12755703 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12755703 | pubmed:pagination | 2476-85 | lld:pubmed |
| pubmed-article:12755703 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
| pubmed-article:12755703 | pubmed:meshHeading | pubmed-meshheading:12755703... | lld:pubmed |
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| pubmed-article:12755703 | pubmed:meshHeading | pubmed-meshheading:12755703... | lld:pubmed |
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| pubmed-article:12755703 | pubmed:meshHeading | pubmed-meshheading:12755703... | lld:pubmed |
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| pubmed-article:12755703 | pubmed:meshHeading | pubmed-meshheading:12755703... | lld:pubmed |
| pubmed-article:12755703 | pubmed:meshHeading | pubmed-meshheading:12755703... | lld:pubmed |
| pubmed-article:12755703 | pubmed:meshHeading | pubmed-meshheading:12755703... | lld:pubmed |
| pubmed-article:12755703 | pubmed:meshHeading | pubmed-meshheading:12755703... | lld:pubmed |
| pubmed-article:12755703 | pubmed:meshHeading | pubmed-meshheading:12755703... | lld:pubmed |
| pubmed-article:12755703 | pubmed:meshHeading | pubmed-meshheading:12755703... | lld:pubmed |
| pubmed-article:12755703 | pubmed:meshHeading | pubmed-meshheading:12755703... | lld:pubmed |
| pubmed-article:12755703 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12755703 | pubmed:articleTitle | Two W-containing formate dehydrogenases (CO2-reductases) involved in syntrophic propionate oxidation by Syntrophobacter fumaroxidans. | lld:pubmed |
| pubmed-article:12755703 | pubmed:affiliation | Laboratory of Microbiology, Wageningen University, The Netherlands. Frank.deBok@wur.nl | lld:pubmed |
| pubmed-article:12755703 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12755703 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12755703 | lld:pubmed |
