Multiband echo tomography of Sco X-1

We present preliminary results of a simultaneous X-ray/optical campaign of the prototypical LMXB Sco X-1 at 1–10 Hz time resolution. Lightcurves of the high excitation Bowen/HeII emission lines and a red continuum at λ_c  6000 Å were obtained through narrow interference filters with ULTRACAM, and these were cross-correlated with simultaneous RXTE X-ray lightcurves. We find evidence for correlated variability, in particular when Sco X-1 enters the Flaring branch. The Bowen/HeII lightcurves lag the X-ray lightcurves with a light travel time which is consistent with reprocessing in the companion star while the continuum lightcurves have shorter delays consistent with reprocessing in the accretion disc.     

Domain evolution and functional diversification of sulfite reductases

Sulfite reductases are key enzymes of assimilatory and dissimilatory sulfur metabolism, which occur in diverse bacterial and archaeal lineages. They share a highly conserved domain "C-X5-C-n-C-X3-C" for binding siroheme and iron-sulfur clusters that facilitate electron transfer to the substrate. For each sulfite reductase cluster, the siroheme-binding domain is positioned slightly differently at the N-terminus of dsrA and dsrB, while in the assimilatory proteins the siroheme domain is located at the C-terminus. Our sequence and phylogenetic analysis of the siroheme-binding domain shows that sulfite reductase sequences diverged from a common ancestor into four separate clusters (aSir, alSir, dsr, and asrC) that are biochemically distinct; each serves a different assimilatory or dissimilatory role in sulfur metabolism. The phylogenetic distribution and functional grouping in sulfite reductase clusters (dsrA and dsrB vs. aSiR, asrC, and alSir) suggest that their functional diversification during evolution may have preceded the bacterial/archaeal divergence.