A wide variety of stresses have been proposed to exert killing effects upon bacteria by stimulating the intracellular formation of reactive oxygen species (ROS). A key part of the supporting evidence has often been the ability of antioxidant compounds to protect the cells. In this study, some of the most-used antioxidants-thiourea, glutathione, N-acetylcysteine, and ascorbate-have been examined.
View Article and Find Full Text PDFThe structure of free cysteine makes it vulnerable to oxidation by molecular oxygen; consequently, organisms that live in oxic habitats have acquired the ability to import cystine as a sulfur source. We show that cystine imported into Escherichia coli can transfer disulfide bonds to cytoplasmic proteins. To minimize this problem, the imported cystine is rapidly reduced.
View Article and Find Full Text PDFBacteria release cysteine to moderate the size of their intracellular pools. They can also evolve hydrogen sulfide, either through dissimilatory reduction of oxidized forms of sulfur or through the deliberate or inadvertent degradation of intracellular cysteine. These processes can have important consequences upon microbial communities, because excreted cysteine autoxidizes to generate hydrogen peroxide, and hydrogen sulfide is a potentially toxic species that can block aerobic respiration by inhibiting cytochrome oxidases.
View Article and Find Full Text PDFUsing a specially designed Monte Carlo algorithm with directed loops, we investigate the triangular lattice Ising antiferromagnet with coupling beyond the nearest neighbors. We show that the first-order transition from the stripe state to the paramagnet can be split, giving rise to an intermediate nematic phase in which algebraic correlations coexist with a broken symmetry. Furthermore, we demonstrate the emergence of several properties of a more topological nature such as fractional edge excitations in the stripe state, the proliferation of double domain walls in the nematic phase, and the Kasteleyn transition between them.
View Article and Find Full Text PDFWhen sulfur compounds are scarce or difficult to process, Escherichia coli adapts by inducing the high-level expression of sulfur-compound importers. If cystine then becomes available, the cystine is rapidly overimported and reduced, leading to a burgeoning pool of intracellular cysteine. Most of the excess cysteine is exported, but some is adventitiously degraded, with the consequent release of sulfide.
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