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Damborský J 《Folia microbiologica》1999,44(3):247-262
Tetrachloroethene is a frequent groundwater contaminant often persisting in the subsurface environments. It is recalcitrant under aerobic conditions because it is in a highly oxidized state and is not readily susceptible to oxidation. Nevertheless, at least 15 organisms from different metabolic groups, viz. halorespirators (9), acetogens (2), methanogens (3) and facultative anaerobes (2), that are able to metabolize tetrachloroethene have been isolated as axenic cultures to-date. Some of these organisms couple dehalo-genation to energy conservation and utilize tetrachloroethene as the only source of energy while others dehalogenate tetrachloroethene fortuitously. Halorespiring organisms (halorespirators) utilize halogenated organic compounds as electron acceptors in an anaerobic respiratory process. Different organisms exhibit differences in the final products of tetrachloroethene dehalogenation, some strains convert tetrachloroethene to trichloroethene only, while others also carry out consecutive dehalogenation to dichloroethenes and vinyl chloride. Thus far, only a single organism, 'Dehalococcoides ethenogenes' strain 195, has been isolated which dechlorinates tetrachloroethene all the way down to ethylene. The majority of tetrachloroethene-dehalogenating organisms have been isolated only in the past few years and several of them, i.e., Dehalobacter restrictus, Desulfitobacterium dehalogenans, 'Dehalococcoides ethenogenes', 'Dehalospirillum multivorans', Desulfuromonas chloroethenica, and Desulfomonile tiedjei, are representatives of new taxonomic groups. This contribution summarizes the available information regarding the axenic cultures of the tetrachloroethene-dehalogenating bacteria. The present knowledge about the isolation of these organisms, their physiological characteristics, morphology, taxonomy and their ability to dechlorinate tetrachloroethene is presented to facilitate a comprehensive comparison. 相似文献
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Urease activity of adherent bacteria and rumen fluid bacteria 总被引:1,自引:0,他引:1
In experiments on six sheep fed on a low nitrogen diet (3.7 g N/day), urease (EC 3.5.1.5) activity (nkat X mg-1 bacterial dry weight) 3 h after feeding was found to be highest in the bacteria adhering to the rumen wall (13.25 +/- 2.10), lower in the rumen fluid bacteria (8.96 +/- 1.35) and lowest in the bacteria adhering to feed particles in the rumen (5.69 +/- 2.13). The urease activity of bacteria adhering to the rumen wall and of the rumen fluid bacteria of six sheep fed on a high nitrogen diet (21 g N/day) was significantly lower than in sheep with a low N intake and in both cases was roughly the same (3.81 +/- 1.37 and 3.76 +/- 1.02 respectively); it was lowest in bacteria adhering to feed particles in the rumen (1.92 +/- 0.90). It is concluded from the results that the urease activity of rumen fluid bacteria and of bacteria adhering to the rumen wall and to feed particles in the rumen is different and that it falls significantly in the presence of a high nitrogen intake. From the relatively high ureolytic activity of bacteria adhering to the rumen wall in the presence of a low nitrogen intake it is assumed that this is one of the partial mechanisms of the hydrolysis of blood urea entering the rumen across the rumen wall and of its reutilization in the rumen-liver nitrogen cycle in ruminants. 相似文献
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Lipoproteins in bacteria 总被引:78,自引:0,他引:78
Covalent modification of membrane proteins with lipids appears to be ubiquitous in all living cells. The major outer membrane (Braun's) lipoprotein ofE. coli, the prototype of bacterial lipoproteins, is first synthesized as a precursor protein. Analysis of signal sequences of 26 distinct lipoprotein precursors has revealed a consensus sequence of lipoprotein modification/processing site of Leu-(Ala, Ser)-(Gly, Ala)-Cys at – 3 to + 1 positions which would represent the cleavage region of about three-fourth of all lipoprotein signal sequences in bacteria. Unmodified prolipoprotein with the putative consensus sequence undergoes sequential modification and processing reactions catalyzed by glyceryl transferase, O-acyl transferase(s), prolipoprotein signal peptidase (signal peptidase II), and N-acyl transferase to form mature lipoprotein. Like all exported proteins, the export of lipoprotein requires functional SecA, SecY, and SecD proteins. Thus all precursor proteins are exported through a common pathway accessible to both signal peptidase I and signal peptidase II. The rapidly increasing list of lipid-modified proteins in both prokaryotic as well as eukaryotic cells indicates that lipoproteins comprise a diverse group of structurally and functionally distinct proteins. They share a common structural feature which is derived from a common biosynthetic pathway. 相似文献
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The degradation of amino acids in anaerobic digestion was examined in terms of the interactions between amino-acid-degrading bacteria and methanogenic bacteria. Certain amino acids were degraded oxidatively by dehydrogenation, with methanogenic bacteria acting as H(2) acceptors. The inhibition of methanogenesis by chloroform also inhibited the degradation of these amino acids and/or caused variations in the composition of volatile acids produced from them. The presence of glycine reduced the inhibitory effect caused by chloroform, probably because glycine acted as an H(2) acceptor in place of methanogenic bacteria. This fact suggested that the coupled oxidation-reduction reactions between two amino acids-one acting as the H(2) donor and the other acting as the H(2) acceptor-may occur in the anaerobic digestion of proteins or amino-acid mixtures. The conversion of some proteins to volatile acids was not affected when methanogenesis was inhibited by chloroform. This suggested that the component amino acids of proteins may be degraded by the coupled oxidation-reduction reactions and that the degradation of proteins may not be dependent on the activity of methanogenic bacteria as H(2) acceptors. 相似文献