Reduction and removal of heptavalent technetium from solution by Escherichia coli.
Anaerobic, but not aerobic, cultures of Escherichia coli accumulated Tc(VII) and reduced it to a black insoluble precipitate. Tc was the predominant element detected when the precipitate was analyzed by proton-induced X-ray emission. Electron microscopy in combination with energy-dispersive X-ray analysis showed that the site of Tc deposition was intracellular. It is proposed that Tc precipitation was a result of enzymatically mediated reduction of Tc(VII) to an insoluble oxide. Formate was an effective electron donor for Tc(VII) reduction which could be replaced by pyruvate, glucose, or glycerol but not by acetate, lactate, succinate, or ethanol. Mutants defective in the synthesis of the transcription factor FNR, in molybdenum cofactor (molybdopterin guanine dinucleotide [MGD]) synthesis, or in formate dehydrogenase H synthesis were all defective in Tc(VII) reduction, implicating a role for the formate hydrogenlyase complex in Tc(VII) reduction. The following observations confirmed that the hydrogenase III (Hyc) component of formate hydrogenlyase in both essential and sufficient for Tc(VII) reduction: (i) dihydrogen could replace formate as an effective electron donor for Tc(VII) reduction by wild-type bacteria and mutants defective in MGD synthesis; (ii) the inability of fnr mutants to reduce Tc(VII) can be suppressed phenotypically by growth with 250 microM Ni2+ and formate; (iii) Tc(VII) reduction is defective in a hyc mutant; (iv) the ability to reduce Tc(VII) was repressed during anaerobic growth in the presence of nitrate, but this repression was counteracted by the addition of formate to the growth medium; (v) H2, but not formate, was an effective electron donor for a Sel- mutant which is unable to incorporate selenocysteine into any of the three known formate dehydrogenases of E. coli. This appears to be the first report of Hyc functioning as an H2-oxidizing hydrogenase or as a dissimilatory metal ion reductase in enteric bacteria.
Lloyd
J R
JR
School of Biological Sciences, University of Birmingham, Edgbaston, United Kingdom. J.R.Lloyd@BHAM.AC.UK
Cole
J A
JA
Macaskie
L E
LE
D000693:Anaerobiosis; D001426:Bacterial Proteins / Q000378:metabolism; D011232:Chemical Precipitation; D003470:Culture Media; D004579:Electron Transport; D004926:Escherichia coli / Q000378:metabolism* / Q000648:ultrastructure; D029968:Escherichia coli Proteins; D005560:Formate Dehydrogenases / Q000378:metabolism; D005561:Formates / Q000378:metabolism; D006859:Hydrogen / Q000378:metabolism; D006864:Hydrogenase / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000378:metabolism; D008854:Microscopy, Electron; D009097:Multienzyme Complexes / Q000378:metabolism; D009566:Nitrates / Q000378:metabolism; D010084:Oxidation-Reduction; D013670:Sodium Pertechnetate Tc 99m / Q000378:metabolism; D013667:Technetium / Q000378:metabolism*; D014157:Transcription Factors / Q000378:metabolism
D001426:Bacterial Proteins; D003470:Culture Media; D029968:Escherichia coli Proteins; C060704:FNR protein, E coli; D005561:Formates; D007506:Iron-Sulfur Proteins; D009097:Multienzyme Complexes; D009566:Nitrates; D014157:Transcription Factors; C030544:formic acid; D013667:Technetium; D006859:Hydrogen; D013670:Sodium Pertechnetate Tc 99m; D006864:Hydrogenase; D005560:Formate Dehydrogenases; C054017:formate hydrogenlyase