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  • Regulation  (84)
  • Hydrogenase  (75)
  • 1
    ISSN: 1432-072X
    Keywords: Hydrogen bacteria ; Hydrogenase ; Localization ; Membrane bound enzymes ; NAD reduction ; Stability
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Alcaligenes eutrophus strains H 16, B 19, G 27 and N9A contained two different hydrogenases. One enzyme catalyzed the reduction of NAD by hydrogen and was strictly localized in the soluble cell fraction, while the second enzyme was found to be particulate and unable to react with NAD. All other tested strains, Alcaligenes paradoxus SA 29, Pseudomonas facilis, P. palleronii RH 2, Pseudomonas sp. strain GA 3, Paracoccus denitrificans, Aquaspirillum autotrophicum SA 32, and Corynebacterium autotrophicum 14g and 7C contained only a single enzyme exclusively bound to membranes. This was established using fractional centrifugation, indicator enzyme systems, gentle methods of cell disintegration and discontinuous sucrose density gradient centrifugation. In cell-free extracts obtained by rough disruption (sonication) of cells, hydrogenase was associated to particles of different size and sedimentation velocity. A partial solubilization of hydrogenase caused by sonication was observed with P. facilis. Without exception, the particulate hydrogenases were found (1) to be unable to reduce pyridine nucleotides, and (2) to reduce methylene blue at an extremely high activity. The eminent reaction rate of 34 μmoles H2 oxidized per min and mg protein has been determined in particle suspensions of Pseudomonas sp. strain GA 3. All hydrogenases were stable during storage under hydrogen atmosphere, except the soluble enzyme from A. eutrophus H 16 which was shown to be more stable under aerobic conditions.
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 112 (1977), S. 283-285 
    ISSN: 1432-072X
    Keywords: Wine yeasts ; Sulfur metabolism ; Regulation ; Sulfate uptake
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Five different strains of wine yeasts were investigated with respect to active uptake of [35S] sulfate and its regulation by methionine. Considerable differences exist between “low” and “high” sulfite-producing strains in the initial velocity of sulfate uptake. Further differences were established in repression of sulfate permease by l-methionine, most evident in a total lack of repression in one of the “high” sulfite producers. These findings explain in part variable sulfite and sulfide formation.
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  • 3
    ISSN: 1432-072X
    Keywords: cAMP ; Regulation ; Chlorophyll synthesis ; Chlorella fusca
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The intracellular concentration of cAMP in the green alga Chlorella fusca was in the range of 2 · 10-9 to 10-8 moles/g dry weight and was strongly dependent on the growth conditions. The cAMP level was high with high light intensity, low nitrate or glucose concentration. Intracellular cAMP increased only by factor of 2 when high amounts (up to 10-3 M) of cAMP were added to the medium. Most of the given cAMP was converted to 5′-AMP. Addition of cAMP had little effect on the chlorophyll content of the cells, only at 10-6 M some enhancement in photoautotrophic cultures was observed. On the other hand high amounts of cAMP in the medium increased the growth rate. DBcAMP* showed a positive effect on chlorophyll synthesis and growth rate at much lower concentrations compared to cAMP. Stimulation effects of exogenous cAMP on the synthesis of chlorophyll were also observed in mixotrophic cultures with a high glucose/nitrate ratio, conditions where chlorophyll synthesis is repressed. Similar to autotrophic conditions DBcAMP was more effective than cAMP. These data indicate that cAMP may act in a system controlling the chlorophyll content of the cells in response to nutrients or light.
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  • 4
    ISSN: 1432-072X
    Keywords: Root nodule symbiosis ; Rhizobium meliloti ; Medicago sativa ; Nitrogenase activity ; Regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Symbiotic nitrogen fixation of Rhizobium meliloti bacteroids in Medicago sativa root nodules was suppressed by several inorganic nitrogen sources. Amino acids like glutamine, glutamic acid and aspartic acid, which can serve as sole nitrogen sources for the unnodulated plant did not influence nitrogenase activity of effective nodules, even at high concentrations. Ammonia and nitrate suppressed symbiotic nitrogen fixation in vivo only at concentrations much higher than those needed for suppression of nitrogenase activity in free living nitrogen fixing bacteria. The kinetics of suppression were slow compared with that of free living nitrogen fixing bacteria. On the other hand, nitrite, which acts as a direct inhibitor of nitrogenase, suppressed very quickly and at low concentrations. Glutamic acid and glutamine enhanced the effect of ammonia dramatically, while the suppression by nitrate was enhanced only slightly.
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 116 (1978), S. 125-132 
    ISSN: 1432-072X
    Keywords: Heterocyst ; Blue-green algae ; Anabaena ; Nitrogenase ; Hydrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Isolated heterocysts of Anabaena 7120 evolve H2 in an ATP-dependent nitrogenase-catalyzed process that is inhibited by N2 and C2H2. Heterocysts have an active uptake hydrogenase that only requires an electron acceptor of positive redox potential, e.g., methylene blue, dichlorophenolindophenol or potassium ferricyanide. O2 supplied at low partial pressures is a very effective physiological oxidant for H2 uptake. High concentrations of O2 are inhibitory to H2 uptake. The oxyhydrogen reaction in heterocysts appears to be mediated by a cytochrome-cytochrome oxidase system, and it supports ATP synthesis via oxidative phosphorylation. Attempts to demonstrate acetylene reduction in isolated heterocysts employing H2 as an electron donor were unsuccessful. It is suggested that the uptake hydrogenase functions to conserve reductant that otherwise would be dissipated via nitrogenase-catalyzed H2 evolution.
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  • 6
    ISSN: 1432-072X
    Keywords: Physarum polycephalum ; Amoebae ; Aminopeptidases ; Acid proteases ; Regulation ; Development ; Differential gene activity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The cultivation of Physarum polycephalum amoebae in two media with different protein contents revealed a regulation of aminopeptidases and proteases depending on the albumin content of the medium: in growing amoebae and plasmodia the aminopeptidases have similar isoenzyme patterns and relative activities against nitroanilides. One alanine and four leucine aminopeptidase isoenzymes were found within the slightly acid pH range. During growth amoebae secrete—different from plasmodia—leucine aminopeptidase into the medium with low protein content. In an albumin-rich medium additional alanine aminopeptidase activity was found. Out of nine plasmodial proteases four were found in amoebae too. Only one band (pI 3.6) was present in the protein-poor medium. No protease activity could be detected in the proteinrich medium.
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  • 7
    ISSN: 1432-072X
    Keywords: Cyanobacteria ; Knallgas reaction ; Hydrogenase ; Hydrogen utilization ; Nitrogenase ; Nitrogen fixation ; Isolated heterocysts ; Anabaena cylindrica ; Nostoc muscorum ; Anabaena variabilis ; Anacystis nidulans ; Cyanophora paradoxa
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Several blue-green algae were surveyed for the occurrence of the hydrogenase which was assayed by the oxyhydrogen or Knallgas reaction in the intact organisms. In aerobically grown cultures, the reaction was detectable in Anabaena cylindrica, Nostoc muscorum and in two Anabaena variabilis species, whereas virtually no activity was observed in Anacystis nidulans and Cyanophora paradoxa. In these latter two algae, the reaction was, however, found after growth under molecular hydrogen for several days, which drastically increased the activity levels with all the algae tested. In the nitrogen fixing species, the activity of the Knallgas reaction was enhanced when all combined nitrogen was omitted from the media. H2 and hydrogenase could not significantly support the CO2-fixation in photoreduction experiments with all blue-green algae investigated here. Hydrogenase was assayed by the dithionite and methyl viologen dependent evolution of hydrogen and was found to be present with essentially the same specific activity levels in preparations of both heterocysts and vegetative cells from Anabaena cylindrica. Na2S2O4 as well as H2 supported the C2H2-reduction of the isolated heterocysts. The H2-dependent C2H2-reduction did not require the presence of oxygen but was strictly light-dependent where H2 served as an electron donor to photosystem I of these cells. It is concluded that hydrogen can be utilized by two different pathways in blue-green algae.
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  • 8
    ISSN: 1432-072X
    Keywords: Streptococcus cremoris ; Cell wall proteinase ; Calcium dependency ; Regulation ; Translational control
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The persistent accumulation of proteinase (PIII) activity in the cell wall of Streptococcus cremoris strain AM1 during growth depends on the presence of Ca2+-ions in the medium. In the absence of calcium initial accumulation of activity in the cell wall is observed, followed by a decrease to a low final level. Under this condition no increase of proteolytic activity is found in the extracellular fluid. A possible function of calcium in the stabilization of the enzyme is discussed. Prolonged accumulation of catalytically active proteinase PIII in the cell wall occurs in the absence of messenger ribonucleic acid synthesis. This process involves de novo protein synthesis supported by preformed proteinase-specific messenger ribonucleic acid, which is possibly either intrinsically long-lived or is stabilized following its transcription. The level of the extracellular concentration of amino acids and/or peptides regulates the translation of newly synthesized proteinase-specific messenger ribonucleic acid and, possibly, the growth of the organism in milk.
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  • 9
    ISSN: 1432-072X
    Keywords: Clostridium sp. La 1 ; Carbon sources ; Clostridium kluyveri ; Hydrogenase ; Enoate reductase ; Relationship of enoate reductase and hydrogenase ; Iron ; Sulfur
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The enzyme activities of Clostridium La 1 and Clostridium kluyveri involved in the stereospecific hydrogenation of α,β-unsaturated carbonyl compounds with hydrogen gas were measured. In C. La 1 the specific activities of hydrogenase and enoate reductase depended heavily on the growth phase and the composition of the medium. During growth in batch cultures on 70 mM crotonate the specific activity of hydrogenase increased and then dropped to about 10% of its maximum value, whereas the activity of enoate reductase reached its maximum in cells of the stationary phase. Under certain conditions during growth the activity ratio hydrogenase: enoate reductase changed from 120 to 1. Thus, the rate limiting enzyme for the hydrogenation can be either the hydrogenase or the enoate reductase, depending on the growth conditions of the cells. The specific activities of ferredoxin-NAD reductase and butyryl-CoA dehydrogenase increased 3-4-fold during growth on crotonate. By turbidostatic experiments it was shown that at constant input of high crotonate concentrations (200 mM) the enoate reductase activity was almost completely suppressed; it increased steadily with decreasing crotonate down to an input concentration of 35 mM. Glucose as carbon source led to high hydrogenase and negligible enoate reductase activities. The latter could be induced by changing the carbon source of the medium from glucose to crotonate. Tetracycline inhibited the formation of enoate reductase. A series of other carbon sources was tested. They can be divided into ones which result in high hydrogenase and rather low enoate reductase activities and others which cause the reverse effect. When the Fe2+ concentration in crotonate medium was growth limiting, cells with relatively high hydrogenase activity and very low enoate reductase activity in the stationary phase were obtained. At Fe2+ concentrations above 3·10-7 M enoate reductase increased and hydrogenase activity reached its minimum. The ratio of activities changes by a factor of about 200. In a similar way the dependence of enzyme activities on the concentration of sulfate was studied. In batch cultures of Clostridium kluyveri a similar opposite time course of enoate reductase and hydrogenase was found. The possible physiological significance of this behavior is discussed.
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  • 10
    ISSN: 1432-072X
    Keywords: Collagenase ; Alkaline protease ; Temperature control ; Oxygen control ; Regulation ; Vibrio alginolyticus ; Secretion exoproteins ; Cerulenin ; Quinacrine ; Microbial ecology
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The production of an extracellular collagenase and an alkaline protease by Vibrio alginolyticus during stationary phase was inhibited by a temperature shift from 30 to 37°C and by a lack of oxygen. The stability of the exoproteases was unaffected by incubation at 37°C and aeration. The optimum growth temperature for the V. alginolyticus strain was 33.5°C Aeration enhanced the rate of growth of exponential phase cells. Temperature and oxygen did not affect the growth of stationary phase cells when the exoproteases were being produced. Macromolecular synthesis in stationary phase cells was not affected by temperature. There was no rapid release of the exoproteases after temperature shift down and chloramphenicol inhibited the production of the enzymes when added at time of temperature shift down from 37 to 30°C. The regulation of exoprotease production by temperature and oxygen was specific and has implications regarding the ecology of V. alginolyticus. Cerulenin, quinacrine and O-phenanthroline inhibited the production of the exoproteases.
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