In the Atlantic and Pacific oceans, these clades were only found in warm waters with low Fe and high inorganic P levels. Genomic analysis suggests that at least one of these clades thrives in low Fe environments by scavenging organic-bound Fe, a process previously unknown in Prochlorococcus. Furthermore, the capacity to utilize organic-bound Fe appears to have

been acquired horizontally and may be exchanged among other clades of Prochlorococcus. Finally, one of the single Prochlorococcus Fer-1 mw cells sequenced contained a partial genome of what appears to be a prophage integrated into the genome. The ISME Journal (2013) 7, 184-198; doi:10.1038/ismej.2012.89; published online 16 August 2012″
“To survive in a complex world, it is important that unattended,

but salient, input can still draw one’s attention. In this article, we suggest that posterior alpha oscillations (8-13 Hz) provide a mechanism for prioritizing and ordering unattended visual input according to ‘relevance’. Gamma oscillations (30-100 Hz) that are phase-locked to the alpha oscillations keep competing unattended representations apart in time, thus creating a sequence of perceptual cycles. As inhibition gradually lowers within an alpha cycle, the ordered sequence of competing NSC23766 solubility dmso input is activated, producing a temporal phase code for saliency. The proposed mechanism is based on recent experiments indicating that the phase of alpha activity modulates perception and that alpha SCH727965 mw oscillations are produced by periodic pulses of inhibition.”
“In methanogenic Archaea, the final step of methanogenesis generates

methane and a heterodisulfide of coenzyme M and coenzyme B (CoM-S-S-CoB). Reduction of this heterodisulfide by heterodisulfide reductase to regenerate HS-CoM and HS-CoB is an exergonic process. Thauer et al. [Thauer, et al. 2008 Nat Rev Microbiol 6: 579-591] recently suggested that in hydrogenotrophic methanogens the energy of heterodisulfide reduction powers the most endergonic reaction in the pathway, catalyzed by the formylmethanofuran dehydrogenase, via flavin-based electron bifurcation. Here we present evidence that these two steps in methanogenesis are physically linked. We identify a protein complex from the hydrogenotrophic methanogen, Methanococcus maripaludis, that contains heterodisulfide reductase, formylmethanofuran dehydrogenase, F(420)-nonreducing hydrogenase, and formate dehydrogenase. In addition to establishing a physical basis for the electron-bifurcation model of energy conservation, the composition of the complex also suggests that either H(2) or formate (two alternative electron donors for methanogenesis) can donate electrons to the heterodisulfide-H(2) via F(420)-nonreducing hydrogenase or formate via formate dehydrogenase.