ArticleExtremophiles : life under extreme conditions2009
Characterization of a soluble oxidoreductase from the thermophilic bacterium Carboxydothermus ferrireducens.
Article in Extremophiles : life under extreme conditions, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- The Geoglobus acetivorans genome: Fe(III) reduction, acetate utilization, autotrophic growth, and degradation of aromatic compounds in a hyperthermophilic archaeon.Applied and environmental microbiology · 2015Article
- Complete genome sequence of the chromate-reducing bacterium Thermoanaerobacter thermohydrosulfuricus strain BSB-33.Standards in genomic sciences · 2015Article
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Authors and funding
3 authors.
Funding
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Abstract
An NAD(P)H-dependent oxidoreductase has been purified approximately 40-fold from the soluble protein fraction of the dissimilatory iron-reducing, anaerobic, thermophilic bacterium Carboxydothermus ferrireducens. The enzyme, a flavoprotein, has broad-substrate specificity-reducing Fe(3+), Cr(6+), and AQDS with rates of 0.31, 0.33, and 3.3 U mg(-1) protein and calculated NADH oxidation turnover numbers of 0.25, 0.25, and 2.5 s(-1), respectively. Numerous quinones are reduced via a two-electron transfer from NAD(P)H to quinone, thus participating in managing oxidative stress by avoiding the formation of semiquinone radicals.
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Registered trials
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