Ferric iron reduction by Desulfovibrio vulgaris Hildenborough wild type and energy metabolism mutants.
Desulfovibrio vulgaris Hildenborough wild type and its hyn1, hyd and hmc mutants, lacking genes for periplasmic [NiFe] hydrogenase-1, periplasmic [FeFe] hydrogenase or the transmembrane high molecular weight cytochrome (Hmc) complex, respectively, were able to reduce Fe(III) chelated with nitrilotriacetic acid (NTA), but not insoluble ferric oxide, with lactate as the electron donor. The rate and extent of Fe(III)-NTA reduction followed the order hyn = WT > hmc >> hyd, suggesting that reduction of soluble Fe(III) is a periplasmic process that requires the presence of periplasmic [FeFe] hydrogenase. Reduction of Fe(III)-NTA was not coupled to cell growth. In fact cell concentrations declined when D. vulgaris was incubated with Fe(III)-NTA as the only electron acceptor. Wild type and mutant cells reducing a limiting concentration of sulfate (2 mM), reduced Fe(III)-NTA with similar rates. However, these were similarly incapable of catalyzing subsequent lactate-dependent reduction of Fe(III)-NTA to completion. Periplasmic reduction of Fe(III)-NTA appeared to inhibit the productive, sulfate-reducing metabolism of D. vulgaris, possibly because it prevents the cycling of reducing equivalents needed to achieve a net bioenergetic benefit.
Park
Hyung Soo
HS
Department of Biological Sciences, University of Calgary, Calgary, AB, Canada, T2N 1N4.
Lin
Shiping
S
Voordouw
Gerrit
G
D000880:Anthraquinones / Q000378:metabolism; D016969:Desulfovibrio vulgaris / Q000235:genetics* / Q000378:metabolism*; D004734:Energy Metabolism / Q000235:genetics*; D005290:Ferric Compounds / Q000378:metabolism; D005838:Genotype; D006864:Hydrogenase / Q000378:metabolism; D007501:Iron / Q000378:metabolism*; D009154:Mutation; D010084:Oxidation-Reduction; D013431:Sulfates / Q000378:metabolism
D000880:Anthraquinones; D005290:Ferric Compounds; D013431:Sulfates; C408124:anthraquinone-2,6-disulfonate; C092844:ferric oxyhydroxide; D007501:Iron; D006864:Hydrogenase