Previous Article | Next Article ![]()
Applied and Environmental Microbiology, November 2007, p. 6854-6863, Vol. 73, No. 21
0099-2240/07/$08.00+0 doi:10.1128/AEM.00957-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Polytechnic of Milan, Department of Chemistry, Materials and Chemical Engineering Giulio Natta, Milan, Italy,1 University of Verona, Department of Science and Technology, Laboratories of Microbial Biotechnology and Environmental Microbiology, Verona, Italy,2 University of Tuscia, Department of Environmental Sciences, Viterbo, Italy3
Received 29 April 2007/ Accepted 29 August 2007
Biochemical and proteomic tools have been utilized for investigating the mechanism of action of a new Stenotrophomonas maltophilia strain (SeITE02), a gammaproteobacterium capable of resistance to high concentrations of selenite [SeO32–, Se(IV)], reducing it to nontoxic elemental selenium under aerobic conditions; this strain was previously isolated from a selenite-contaminated mining soil. Biochemical analysis demonstrated that (i) nitrite reductase does not seem to take part in the process of selenite reduction by the bacterial strain SeITE02, although its involvement in this process had been hypothesized in other cases; (ii) nitrite strongly interferes with selenite removal when the two oxyanions (NO2– and SeO32–) are simultaneously present, suggesting that the two reduction/detoxification pathways share a common enzymatic step, probably at the level of cellular transport; (iii) in vitro, selenite reduction does not take place in the membrane or periplasmic fractions but only in the cytoplasm, where maximum activity is exhibited at pH 6.0 in the presence of NADPH; and (iv) glutathione is involved in the selenite reduction mechanism, since inhibition of its synthesis leads to a considerable delay in the onset of reduction. As far as the proteomic findings are concerned, the evidence was reached that 0.2 mM selenite and 16 mM nitrite, when added to the culture medium, caused a significant modulation (ca. 10%, i.e., 96 and 85 protein zones, respectively) of the total proteins visualized in the respective two-dimensional maps. These spots were identified by mass spectrometry analysis and were found to belong to the following functional classes: nucleotide synthesis and metabolism, damaged-protein catabolism, protein and amino acid metabolism, and carbohydrate metabolism along with DNA-related proteins and proteins involved in cell division, oxidative stress, and cell wall synthesis.
Published ahead of print on 7 September 2007.
This article has been cited by other articles:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»