Description of a redox-controlled sulfidostat for the growth of sulfide-oxidizing phototrophs

This paper describes a novel type of continuous culture for the growth of phototrophic sulfur oxidizers under constant concentrations of hydrogen sulfide. The culture maintains a constant concentration of sulfide despite possible variations in external factors likely to affect photosynthetic activity. Variations in biological activity lead to small departures from the steady-state concentration of hydrogen sulfide which result in variations of the redox potential. These changes in redox, monitored through a redox controller, modulate the rate at which the medium is pumped into the culture and therefore govern the dilution rate. As a result, when changes in external factors such as the light supply occur, the dilution rate of the culture adjusts to the new rate of sulfide oxidation, while maintaining a virtually constant concentration of hydrogen sulfide. The system has been successfully tested for an extended period of several weeks and under conditions of shifting illumination (868 to 113, 113 to 23, and 23 to 7 (mu)E(middot)m(sup-2)(middot)s(sup-1)). After changes in illumination, a transition to a new dilution rate started immediately, reaching a new equilibrium in less than 3 h.     

Structural modeling of SoxF protein from Chlorobium tepidum: an approach to understand the molecular basis of thiosulfate oxidation

Microbial redox reactions of inorganic sulfur compounds play a vital role in balancing the turnover of this element in the environment. These vital reactions are carried out by the enzyme system encoded by the sox operon. The central player of the sulfur oxidation biochemistry is the SoxY–Z protein complex. Another protein called SoxF having sulfide dehydrogenase activity has the ability to reactivate the inactivated SoxY–Z protein complex. This SoxF protein is obtained from the sox operon of Chlorobium tepidium. In the present work an attempt has been made to understand the structural details of the activity of SoxF protein. A plausible biochemical mechanism has been predicted regarding the involvement of the SoxF protein in biological sulfur anion oxidation process. Since this is the first report regarding the structural biology of SoxF protein this study may shed light in the hitherto unknown molecular biochemistry of sulfur anion oxidation by sox operon.     

Disproportionation of elemental sulfur by haloalkaliphilic bacteria from soda lakes

Microbial disproportionation of elemental sulfur to sulfide and sulfate is a poorly characterized part of the anoxic sulfur cycle. So far, only a few bacterial strains have been described that can couple this reaction to cell growth. Continuous removal of the produced sulfide, for instance by oxidation and/or precipitation with metal ions such as iron, is essential to keep the reaction exergonic. Hitherto, the process has exclusively been reported for neutrophilic anaerobic bacteria. Here, we report for the first time disproportionation of elemental sulfur by three pure cultures of haloalkaliphilic bacteria isolated from soda lakes: the Deltaproteobacteria Desulfurivibrio alkaliphilus and Desulfurivibrio sp. AMeS2, and a member of the Clostridia, Dethiobacter alkaliphilus. All cultures grew in saline media at pH 10 by sulfur disproportionation in the absence of metals as sulfide scavengers. Our data indicate that polysulfides are the dominant sulfur species under highly alkaline conditions and that they might be disproportionated. Furthermore, we report the first organism (Dt. alkaliphilus) from the class Clostridia that is able to grow by sulfur disproportionation.     

Microbially — related redox changes in a subtropical lake 2. Simulation of metalinmetic conditions in a chemostat

The individual influence of sulfate reducing and brown phototrophic sulfur bacteria from Lake Kinneret on the metalimnetic redox conditions was investigated by simulating the hydrochemical and microbiological conditions in a specially designed chemostat. The results show a strong correlation between measured redox values and the prevailing hydrogen sulfide concentration leading to a linear relationship. Changes in this relationship allowed differentiation between the on-going microbial processes, sulfate reduction and sulfide oxidation. The comparison ofin vitro andin situ redox values shows that the results of the simulation experiments agree with the data previously measured in the metalimnion of Lake Kinneret.     

Carrier of reduced sulfur is a possible role for thiotaurine in symbiotic species from hydrothermal vents with thiotrophic symbionts

Experiments supporting the possible role of the free sulfur-containing amino acid thiotaurine, as a transport and storage compound for sulfide in invertebrates with thiotrophic symbionts are described. The free-living chemotrophic sulfur-oxidising bacterium, Thiobacillus hydrothermalis (strain DSMZ 7121), was used as a model for the symbionts as the actual symbionts have not been obtained in culture.Thiotaurine contains two sulfur atoms, namely the inner sulfone and the outer sulfane sulfur; the latter presents a potential source of reducing equivalents for the symbiont. Nevertheless, we observed no oxidation of thiotaurine when this compound was added to a culture of T. hydrothermalis pre-grown on sulfide. In contrast, when thiotaurine was added to the culture together with an extract of the trophosome of a vestimentiferan tubeworm from the Manus basin, we observed that thiotaurine was oxidised to hypotaurine with concomitant acidification and formation of bacterial biomass. Thus, the trophosome contains an unknown catalytic factor. We suggest that thiotaurine requires reduction prior to oxidation by T. hydrothermalisand that the host may catalyse the conversion of thiotaurine through the glutathione redox couple. This way, the host can accurately control energy delivery (as reduced sulfur) to the symbionts and can therefore control their symbiont biomass.