13 research outputs found

    The bioenergetic role of dioxygen and the terminal oxidase(s) in cyanobacteria

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    AbstractOwing to the release of 13 largely or totally sequenced cyanobacterial genomes (see http://www.kazusa.or.jp/cyano and www.jgi.doe.gov/), it is now possible to critically assess and compare the most neglected aspect of cyanobacterial physiology, i.e., cyanobacterial respiration, also on the grounds of pure molecular biology (gene sequences). While there is little doubt that cyanobacteria (blue-green algae) do form the largest, most diversified and in both evolutionary and ecological respects most significant group of (micro)organisms on our earth, and that what renders our blue planet earth to what it is, viz. the O2-containing atmosphere, dates back to the oxygenic photosynthetic activity of primordial cyanobacteria about 3.2×109 years ago, there is still an amazing lack of knowledge on the second half of bioenergetic oxygen metabolism in cyanobacteria, on (aerobic) respiration. Thus, the purpose of this review is threefold: (1) to point out the unprecedented role of the cyanobacteria for maintaining the delicate steady state of our terrestrial biosphere and atmosphere through a major contribution to the poising of oxygenic photosynthesis against aerobic respiration (“the global biological oxygen cycle”); (2) to briefly highlight the membrane-bound electron-transport assemblies of respiration and photosynthesis in the unique two-membrane system of cyanobacteria (comprising cytoplasmic membrane and intracytoplasmic or thylakoid membranes, without obvious anastomoses between them); and (3) to critically compare the (deduced) amino acid sequences of the multitude of hypothetical terminal oxidases in the nine fully sequenced cyanobacterial species plus four additional species where at least the terminal oxidases were sequenced. These will then be compared with sequences of other proton-pumping haem–copper oxidases, with special emphasis on possible mechanisms of electron and proton transfer

    Research in the field of using of ash from the incineration of sewage sludge, treated with mineral binders, for forest road construction

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    The purpose of the study is to obtain a durable and cheap road-building material based on ash, reinforced with mineral astringent. Within the framework of the research, the optimal dosages of binders were searched for, the characteristics of the strength of mixture of ash with sludge and ash with cement were also determined. A comparative analysis of the economic efficiency between using a mixture of ash from the incineration of sewage sludge, reinforced with nepheline sludge, and traditional road building materials was carried out. The results of the study of mixtures of ash with mineral binders, such as nepheline sludge and cement, show that the obtained materials have high strength indicators and high indicators of the modulus of elasticity. They can be attributed to strength grades from M20 to M100. The developed building material (ash mixed with binders (nepheline sludge, cement)) could replace a similar building material in the technology of road construction, because if this mixture is taken in optimal dosages, it will be more profitable in the process of use, both from the point of physical and mechanical views, and point of view of economic indicators

    Time-resolved generation of a membrane potential by ba(3) cytochrome c oxidase from Thermus thermophilus - Evidence for reduction-induced opening of the binuclear center

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    Abstractba3-type cytochrome c oxidase purified from the thermophilic bacterium Thermus thermophilus has been reconstituted in phospholipid vesicles and laser flash-induced generation of a membrane potential by the enzyme has been studied in a ÎŒs/ms time scale with Ru(II)-tris-bipyridyl complex (RuBpy) as a photoreductant. Flash-induced single electron reduction of the aerobically oxidized ba3 by RuBpy results in two phases of membrane potential generation by the enzyme with τ values of about 20 and 300 ÎŒs at pH 8 and 23°C. Spectrophotometric experiments show that oxidized ba3 reacts very poorly with hydrogen peroxide or any of the other exogenous heme iron ligands studied like cyanide, sulfide and azide. At the same time, photoreduction of the enzyme by RuBpy triggers the electrogenic reaction with H2O2 with a second order rate constant of ∌2×103 M−1 s−1. The data indicate that single electron reduction of ba3 oxidase opens the binuclear center of the enzyme for exogenous ligands. The fractional contribution of the protonic electrogenic phases induced by peroxide in cytochrome ba3 is much less than in bovine oxidase, pointing to a possibility of a different electrogenic mechanism of the ba3 oxidase as compared to the oxidases of the aa3-type
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