Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.12.7.2 (hydrogenase)
3,522 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

When Rhodopseudomonas capsulata B10 grows in media with different organic compounds, the hydrogenase activity estimated both by the evolution and uptake of H2 is lowest in cells taken from the middle of the exponential growth phase, and highest in cells from the beginning of the stationary phase. Cells grown in a medium containing malate have a higher hydrogenase activity than those cultivated in a medium with lactate or other compounds (900 and 20 nmoles of H2 per 1 min per 1 mg of protein, respectively). In the experiments with chloramphenicol (10(-5) M), organic compounds (not CO2) were shown to repress hydrogenase synthesis. When the cells were incubated in a medium without an organic substrate or in its presence, the exogenous H2 or H2 evolved as the result of nitrogenase action causes an increase in the activity of hydrogenase.
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PMID:[Hydrogenase activity of Rhodopseudomonas capsulata growing on organic media]. 675 94

An evolutionary explanation is sought for the fact that ATP is needed for N2 fixation in spite of the exergonicity of the process. After a survey of the state of knowledge about the thermodynamics of N2 fixation in fermenters, photosynthesizers and respirers it is suggested that nitrogenase, which still shows ATP-dependent hydrogenase activity, evolved from an ATP-requiring hydrogenase that lacked nitrogenase activity. The hydrogenase action in the Archaean, reducing, biosphere may have needed ATP to ensure expulsion of H2. Extant non-nitrogenase hydrogenases have lost the dependence on ATP. Because of its complexity, nitrogenase could not rid itself of the ATP dependence or of hydrogenase activity, both wasteful. Presumably all hydrogenases evoled from ferredoxin-like Fe-S proteins.
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PMID:Evolutionary considerations on the thermodynamics of nitrogen fixation. 677 99

Two H2 uptake-negative (Hup-) Rhizobium japonicum mutants were obtained that also lacked symbiotic N2 fixation (acetylene reduction) activity. One of the mutants formed green nodules and was deficient in heme. Hydrogen oxidation activity in this mutant could be restored by the addition of heme plus ATP to crude extracts. Bacteroid extracts from the other mutant strain lacked hydrogenase activity and activity for both of the nitrogenase component proteins. Hup+ revertants of the mutant strains regained both H2 uptake ability and nitrogenase activity.
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PMID:Nif- Hup- mutants of Rhizobium japonicum. 687 48

The greatest rate of acetylene reduction by Rhodopseudomonas spheroides and Rhodopseudomonas capsulata strains was found in the light in the presence of pyruvate, malate or lactate as well as, in the case of Rh. capsulata, in the presence of 10% H2. The activity of nitrogenase was higher in cells grown in the medium with malate than in cells cultivated in the medium with lactate. All the three strains of Rh. spheroides were characterized by a direct correlation between the rates of H2 photoproduction and C2H2 photoreduction. Such a correlation was not found for Rh. capsulata strains. This can be attributed to the fact that Rh. capsulata strains capable of effective H2 uptake utilize hydrogen evolved in the light in the presence of nitrogenase from organic substrates in order to reduce endogenous electron acceptors or acetylene, i.e. its recyclization takes place. In contrast to Rh. capsulata, Rh. spheroides cells exhibit a weaker hydrogenase activity measured in terms of hydrogen evolution and hydrogen uptake. The uptake of H2 is most active at the account of endogenous H-acceptors or in the presence of benzyl viologen and methylene blue but not methyl viologen.
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PMID:[Nitrogenase and hydrogenase activities of the non-sulfur purple bacteria, Rhodopseudomonas spheroides and Rhodopseudomonas capsulata]. 699 15

Hydrogenase activity was found in cells of Rhodopseudomonas capsulata strain B10 cultured under a variety of growth conditions either anaerobically in the light or aerobically in the dark. The highest activities were found routinely in cells grown in the presence of H2. The hydrogenase of R. capsulata was localized in the particulate fraction of the cells. High hydrogenase activities were usually observed in cells possessing an active nitrogenase. The hydrogen produced by the nitrogenase stimulated the activity of hydrogenase in growing cells. However, the synthesis of hydrogenase was not closely linked to the synthesis of nitrogenase. Hydrogenase was present in dark-grown cultures, whereas nitrogenase synthesis was not significant in the absence of light. Unlike nitrogenase, hydrogenase was present in cultures grown on NH4+. Conditions were established which allowed the synthesis of either nitrogenase or hydrogenase by resting cells. We concluded that hydrogenase can be synthesized independently of nitrogenase.
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PMID:Hydrogenase activity in Rhodopseudomonas capsulata: relationship with nitrogenase activity. 699 43

Hydrogen evolution and consumption by cell and chromatophore suspensions of the photosynthetic bacterium Rhodopseudomonas capsulata was measured with a sensitive and specific mass spectrometric technique which directly monitors dissolved gases. H2 production by nitrogenase was inhibited by acetylene and restored by carbon monoxide. An H2 evolution activity coupled with HD formation and D2 uptake (H-D exchange) was unaffected by C2H2 and CO. Cultures lacking nitrogenase activity also exhibited H-D exchange activity, which was catalyzed by a membrane-bound hydrogenase present in the chromatophores of R. capsulata. A net hydrogen uptake, mediated by hydrogenase, was observed when electron acceptors such as CO2, O2, or ferricyanide were present in the medium.
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PMID:Continuous monitoring, by mass spectrometry, of H2 production and recycling in Rhodopseudomonas capsulata. 700 56

The role of uptake hydrogenase was studied in Rhizobium leguminosarum bacteroids from the nodules of Pisum sativum L. cv. Homesteader. Uptake hydrogenase activity, measured by the 3H2 uptake method, was dependent on O-consumption and was similar to H2 uptake measured by gas chromatography. Km for O2 of 0.0007 atm (0.0709 kPa) and a Km for H2 of 0.0074 atm (0.7498, kPa) were determined. H2 increased the rate of endogenous respiration by isolates with uptake hydrogenase (Hup+) but had no effect on an isolate lacking uptake hydrogenase (Hup-). A survey of 14 Hup+ isolates indicated a wide range of H2 uptake activities. Four of the isolates tested had activities similar to or higher than those found in two Hup+ Rhizobium japonicum strains. H2 uptake was strongly coupled to ATP formation in only 5 of the 14 isolates. H2 increased the optimal O2 level of C2H2 reduction by 0.01 atm and permitted enhanced C2H2 reduction at O2 levels above the optimum in both a coupled and an uncoupled isolate. At suboptimal O2 concentrations a small enhancement of C2H2 reduction by H2 was seen in two out of three isolates in which H2 oxidation was coupled to ATP formation. Thus, the main function of uptake hydrogenase in R. leguminosarum appears to be in the protection of nitrogenase from O2 damage.
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PMID:Uptake hydrogenase activity and ATP formation in Rhizobium leguminosarum bacteroids. 704 3

The molybdenum-iron-sulphur cluster [Fe6Mo2S8(SCH2CH2OH)9]3-, which contains two Fe3MoS4 cubane-like centres, is the best plausible analogue available to date for the molybdenum site of the nitrogenase enzymes. The iron-sulphur cluster [Fe4S4(S . CH2CH2OH)4]2- and the iron-selenium cluster [Fe4Se4(S . CH2CH2OH)4]2- are structural analogues of the ferredoxin Fe4S4 active centre. All three clusters would replace ferredoxin and mediate electron transfer to Clostridium pasteurianum hydrogenase in a H2-evolving system with sodium dithionite as the electron donor. The clusters would not replace hydrogenases which themselves are unable to evolve H2 from reduced ferredoxins. The molybdenum-iron-sulphur cluster would also replace ferredoxin in a chloroplast-ferredoxin-hydrogenase H2 evolving system.
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PMID:Biological activity of synthetic molybdenum-iron-sulphur, iron-sulphur and iron-selenium analogues of ferredoxin-type centres. 735 74

The presumed beneficial effect of hydrogenase on growth of diazotrophic bacteria was reinvestigated with carbon-limited chemostat cultures of the hydrogenase-deficient mutant hoxKG of Azotobacter vinelandii and its parent. The results revealed that hydrogen recycling was too low to benefit the cellular energy metabolism or activities of nitrogenase and respiration.
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PMID:Hydrogenase does not confer significant benefits to Azotobacter vinelandii growing diazotrophically under conditions of glucose limitation. 759 61

In Rhodobacter capsulatus, the hupL gene encoding the large subunit of the uptake-hydrogenase (Hup) enzyme complex was mutated by insertion of an interposon. The mutant neither synthesized an active hydrogenase nor grew photoautotrophically. Under conditions of nitrogen (N) limitation, photoheterotrophic cultures of the wild type and the mutant evolved H2 by activity of the nitrogenase enzyme complex. When grown with glutamate as an N source and either D,L-malate or L-lactate as carbon sources, the efficiency of H2 production by the HupL mutant was higher than 90%, whereas wild-type cultures exhibited efficiencies of 54% (with D,L-malate) and 64% (with L-lactate), respectively. With NH4+ as the N source, efficiencies of H2 production were 70% (mutant) and 52% (wild type).
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PMID:Optimizing photoheterotrophic H2 production by Rhodobacter capsulatus upon interposon mutagenesis in the hupL gene. 776 18


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