Discrete sources as the origin of the Galactic X-ray ridge emission

An unresolved X-ray glow (at energies above a few kiloelectronvolts) was discovered about 25 years ago and found to be coincident with the Galactic disk -the Galactic ridge X-ray emission. This emission has a spectrum characteristic of a 1e8 K optically thin thermal plasma, with a prominent iron emission line at 6.7 keV. The gravitational well of the Galactic disk, however, is far too shallow to confine such a hot interstellar medium; instead, it would flow away at a velocity of a few thousand kilometres per second, exceeding the speed of sound in gas. To replenish the energy losses requires a source of 10^{43} erg/s, exceeding by orders of magnitude all plausible energy sources in the Milky Way. An alternative is that the hot plasma is bound to a multitude of faint sources, which is supported by the recently observed similarities in the X-ray and near-infrared surface brightness distributions (the latter traces the Galactic stellar distribution). Here we report that at energies of 6-7 keV, more than 80 per cent of the seemingly diffuse X-ray emission is resolved into discrete sources, probably accreting white dwarfs and coronally active stars.Comment: 16 pages, 3 figures. Draft version of the paper that will appear in Nature, Issue April 30, 200

Ligand Binding Study of Human PEBP1/RKIP: Interaction with Nucleotides and Raf-1 Peptides Evidenced by NMR and Mass Spectrometry

Background Human Phosphatidylethanolamine binding protein 1 (hPEBP1) also known as Raf kinase inhibitory protein (RKIP), affects various cellular processes, and is implicated in metastasis formation and Alzheimer's disease. Human PEBP1 has also been shown to inhibit the Raf/MEK/ERK pathway. Numerous reports concern various mammalian PEBP1 binding ligands. However, since PEBP1 proteins from many different species were investigated, drawing general conclusions regarding human PEBP1 binding properties is rather difficult. Moreover, the binding site of Raf-1 on hPEBP1 is still unknown. Methods/Findings In the present study, we investigated human PEBP1 by NMR to determine the binding site of four different ligands: GTP, FMN, and one Raf-1 peptide in tri-phosphorylated and non-phosphorylated forms. The study was carried out by NMR in near physiological conditions, allowing for the identification of the binding site and the determination of the affinity constants KD for different ligands. Native mass spectrometry was used as an alternative method for measuring KD values. Conclusions/Significance Our study demonstrates and/or confirms the binding of hPEBP1 to the four studied ligands. All of them bind to the same region centered on the conserved ligand-binding pocket of hPEBP1. Although the affinities for GTP and FMN decrease as pH, salt concentration and temperature increase from pH 6.5/NaCl 0 mM/20°C to pH 7.5/NaCl 100 mM/30°C, both ligands clearly do bind under conditions similar to what is found in cells regarding pH, salt concentration and temperature. In addition, our work confirms that residues in the vicinity of the pocket rather than those within the pocket seem to be required for interaction with Raf-1.METASU