Characterization of a soluble oxidoreductase from the thermophilic bacterium Carboxydothermus ferrireducens |
| |
| Authors: | Rob Uche Onyenwoke R Geyer Juergen Wiegel |
| |
| Institution: | (1) Department of Microbiology, The University of Georgia, 212 Biological Sciences Bldg, 1000 Cedar Street, Athens, GA 30602, USA;(2) LC-MS Support, Core Pharma-Central Europe, Applera Europe B.V., Rotkreuz Branch, Grundstrasse 10, 6343 Rotkreuz, Switzerland;(3) Present address: Neuroscience Center, UNC School of Medicine, University of North Carolina, Chapel Hill, NC, USA |
| |
| 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 Fe3+, Cr6+, 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. |
| |
| Keywords: | Anaerobic bacteria Biochemical characterization Thermophiles and thermophilic enzymes Oxidoreductase Metal reduction Oxidative stress Gram-type positive Flavoprotein Quinones |
| 本文献已被 SpringerLink 等数据库收录！ |
|
