However, the mechanism by which NO generates DNA-methylating agents is still unclear. The functions of YeaR and YoaG are unknown, learn more and no clear phenotype has yet been found for a mutant deleted for the yeaR yoaG operon (Squire et al., 2009; C.E. Vine & J.A. Cole, unpublished

data). Unexplained is why the promoter for yeaR transcription is far more active during anaerobic growth than during aerobic growth, and more active in the absence of FNR than in its presence, despite the absence of an FNR site in the regulatory region. Consequently, despite similarities in how the synthesis of these two proteins is regulated, no link has been established between their functions. They are likely to provide protection against side products generated during anaerobic growth when nitrate is abundant. The NsrR-regulated ytfE, hmpA, and ygbA transcripts are more abundant in an fnr mutant than in an fnr+ strain (Bodenmiller & Spiro, 2006). Only the hmpA promoter binds FNR specifically (Cruz-Ramos et al., 2002). Are the others regulated via an FNR-regulated small RNA? The hybrid cluster protein, also known as the prismane protein, has attracted the attention of biochemists for more than two decades because its structure

Lenvatinib is so far unique. It contains two redox-active iron-sulfur clusters. One of them is a conventional [2Fe-2S] cluster, but the other is a [4Fe-2S-2O] cluster (van den Berg et al., 2000). Does its unique structure imply a unique function? According to dogma, which is being reinforced by annotations in genome databases, Hcp is a hydroxylamine reductase that protects bacteria against the toxicity of hydroxylamine generated during nitrite reduction to ammonia. Evidence for

this assumption is based on the ability of Hcp purified from E. coli, Pyrococcus furiosus, and Rhodobacter capsulatus E1F1 to catalyze the reduction of hydroxylamine to ammonia using electrons from NADH or NADPH (Wolfe et al., 2002; Cabello et al., 2004; selleck screening library Overeijnder et al., 2009). Note, however, that these authors were careful not to assume that hydroxylamine is the natural substrate because the catalytic efficiency of this reaction is extremely low. At neutral pH the Km for hydroxylamine is almost three orders of magnitude greater than the concentration that is totally growth-inhibitory, so other roles for Hcp are being considered. Whole genome transcriptomic studies have consistently revealed that expression of the NsrR-regulated hcp gene in E. coli is strongly up-regulated under conditions of nitrosative stress. This suggests that Hcp is more likely to play a currently unidentified role in protecting bacteria from nitrosative stress than by functioning as a specialized hydroxylamine reductase. There appears to be a barrier that prevents the equilibration of external NO across the cytoplasmic membrane (Vine et al., 2011): this barrier remains to be identified.