Similar to M. capsulatus Bath, expression of haoA from M. album ATCC 33003 was unaffected during growth in media amended with 2.5 mM selleck NaNO2 (Fig. 2a). The nirB-containing gene cluster (MCA0588-MCA0594) encodes proteins facilitating uptake and reduction of NO3− to NH4+ for assimilation. Upregulation of such genes by SNP has not been reported for other bacteria, likely because prior studies focused on bacteria that express dissimilatory nitrite reductase. The observation of

an increased nirB transcript in response to SNP but not to NaNO2 remains an unexplained phenomenon. Only incubations of M. capsulatus Bath in NMS (with CH4) amended with NH3 and NO2− together produced N2O at 9.6±1.7 and 26.3±4.3 μM headspace concentration after 24 and 48 h, respectively. N2O was below detection in incubations with SNP alone, NO2− alone, NH3 alone, or SNP plus NH3. Because NH3 induces expression of haoAB and cytS (Poret-Peterson et al., 2008) and NO2− induced norCB expression (Fig. 3),

we conclude that these genes together encode the required inventory for the formation of N2O in M. capsulatus Bath and that this activity requires the presence of both NH3 and NO2− together. In this study, we demonstrated the regulation and implied the function of gene products for NH2OH oxidation by M. album (i.e. haoA) and N2O production by M. capsulatus Bath, although biochemical tests must still be performed to validate these putative functions. The widespread presence and diverse combinations of NH2OH oxidation and

NOx transformation genes among the MOB suggests that multiple pathways catalyze these Anti-infection Compound Library processes. This work was supported by the KY Science and Engineering Foundation grant KSEF-787- RDE-007 (ATPP), incentive funds from the University of Louisville VP Research office (M.A.C., Farnesyltransferase M.G.K.) the Kearney Foundation of Soil Science Grant #2005.202 (L.Y.S.), NSERC (L.Y.S.), and NSF grant EF-0412129 (M.G.K.). The work conducted by the US Department of Energy Joint Genome Institute is supported by the Office of Science of the US Department of Energy under Contract No. DE-AC02-05CH11231. M.A.C., G.N., J.A.K. and A.T.P. contributed equally to this work. Table S1. Oligonucleotide primers used in this study. Please note: Wiley-Blackwell is not responsible for the content or functionality of any supporting materials supplied by the authors. Any queries (other than missing material) should be directed to the corresponding author for the article. “
“Magnetotactic bacteria use a specific set of conserved proteins to biomineralize crystals of magnetite or greigite within their cells in organelles called magnetosomes. Using Magnetospirillum magneticum AMB-1, we examined one of the magnetotactic bacteria-specific conserved proteins named MamP that was recently reported as a new type of cytochrome c that has iron oxidase activity.