Spot evolution in the eclipsing binary CoRoT 105895502

Stellar activity is ubiquitous in late-type stars. The special geometry of eclipsing binary systems is particularly advantageous to study the stellar surfaces and activity. We present a detailed study of the 145 d CoRoT light curve of the short-period eclipsing binary CoRoT 105895502. By means of light-curve modeling with Nightfall, we determine the orbital period, effective temperature, Roche-lobe filling factors, mass ratio, and orbital inclination of CoRoT 105895502 and analyze the temporal behavior of starspots in the system. Our analysis shows one comparably short-lived (about 40 d) starspot, remaining quasi-stationary in the binary frame, and one starspot showing prograde motion at a rate of 2.3 deg per day, whose lifetime exceeds the duration of the observation. In the CoRoT band, starspots account for as much as 0.6 % of the quadrature flux of CoRoT 105895502, however we cannot attribute the spots to individual binary components with certainty. Our findings can be explained by differential rotation, asynchronous stellar rotation, or systematic spot evolution.Comment: Accepted in A&

(Per)chlorate reduction by an acetogenic bacterium, Sporomusa sp., isolated from an underground gas storage

A mesophilic bacterium, strain An4, was isolated from an underground gas storage reservoir with methanol as substrate and perchlorate as electron acceptor. Cells were Gram-negative, spore-forming, straight to curved rods, 0.5–0.8 μm in diameter, and 2–8 μm in length, growing as single cells or in pairs. The cells grew optimally at 37°C, and the pH optimum was around 7. Strain An4 converted various alcohols, organic acids, fructose, acetoin, and H2/CO2 to acetate, usually as the only product. Succinate was decarboxylated to propionate. The isolate was able to respire with (per)chlorate, nitrate, and CO2. The G+C content of the DNA was 42.6 mol%. Based on the 16S rRNA gene sequence analysis, strain An4 was most closely related to Sporomusa ovata (98% similarity). The bacterium reduced perchlorate and chlorate completely to chloride. Key enzymes, perchlorate reductase and chlorite dismutase, were detected in cell-free extracts

Characterization of a Heme-Dependent Catalase from Methanobrevibacter arboriphilus

Recently it was reported that methanogens of the genus Methanobrevibacter exhibit catalase activity. This was surprising, since Methanobrevibacter species belong to the order Methanobacteriales, which are known not to contain cytochromes and to lack the ability to synthesize heme. We report here that Methanobrevibacter arboriphilus strains AZ and DH1 contained catalase activity only when the growth medium was supplemented with hemin. The heme catalase was purified and characterized, and the encoding gene was cloned. The amino acid sequence of the catalase from the methanogens is most similar to that of Methanosarcina barkeri