Inorganic electron acceptors Due to their poor solubility in water, metal-oxides and

-hydroxides [such as Fe(III), Mn(III)/(IV)] are challenging substrates for bacterial respiration. Multiheme c-type cytochromes were shown to mediate dissimilatory reduction of Fe(III) and Mn(III)/(IV) in the Gram-negative bacteria S. oneidensis MR-1- and G. sulfurreducens [32–34]. The Gram-positive D. hafniense DCB-2 contains no homolog for the multiheme cytochromes but is capable of reducing Fe(III) for energy generation [5, 25]. Only three genes potentially encoding c-type cytochromes that are not part of known enzyme systems were identified and none of them had a multiheme motif. Total genome transcriptomic studies have generated a few potential candidates for a dissimilatory Fe(III) reductase. Among them, an operon encoding a molybdopterin oxidoreductase gene (Dhaf_1509) is of particular interest this website since we found a very high level CX-5461 cost of expression (~40 fold) specifically induced when Fe(III) was the terminal electron acceptor. The operon appears to contain six genes including two rhodanese-family genes, a 4Fe-4S binding domain gene, a polysulphide reductase gene, and a TorD- like chaperone

gene (Dhaf_1508-1513). In addition, a decacistronic operon (Dhaf_3547-3556) encoding type IV pilus biosynthesis genes was induced 2-3 fold. In Geobacter sulfurreducens, type IV pilus has been implicated in mediating electron transfer from the cell surface to insoluble Fe(III) [35]. A check details mutant defective in the pilin subunit gene (pilA) could not reduce insoluble ferric oxide but was still able to reduce soluble ferric citrate [35]. In our microarray studies, ferric citrate [Fe(III)] and uranyl acetate [U(VI)] Carnitine palmitoyltransferase II induced the type IV pilus biosynthesis operon, but sodium selenate [Se(VI)] did not [25]. Uranium in nuclear waste poses an ecological and human health hazard. Microbial reduction of soluble U(VI) to U(IV) which precipitates

as uraninite, has been proposed as a method for the immobilization of uranium in situ [36]. Desulfovibrio desulfuricans G20 and Desulfovibrio vulgaris have been shown to directly reduce U(VI), without the involvement of a respiratory electron transfer [37–39]. Similar to the case of Fe(III) reduction, multiheme c-type cytochromes have been postulated in association with U(VI) reduction [38, 39]. As an additional mechanism to explain the reduction of cytoplasmic U(VI) in D. desulfuricans G20, thioredoxin was proposed to be responsible [40]. D. hafniense DCB-2 could reduce U(VI) to U(IV) when pyruvate was provided [25]. Under these conditions, cell growth was significantly inhibited, and long, undivided cells were formed, suggesting that U(VI)/U(IV) is deleterious to cell division. Lactate also supported the cell’s growth on U(VI) but it took much longer (a few months) before the growth reached a detectable level [25].