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)

In the diazotroph Klebsiella pneumoniae the flavoprotein NifL inhibits the activity of the nif-specific transcriptional activator NifA in response to molecular oxygen and combined nitrogen. Sequestration of reduced NifL to the cytoplasmic membrane under anaerobic and nitrogen-limited conditions impairs inhibition of cytoplasmic NifA by NifL. To analyze whether NifL is reduced by electrons directly derived from the reduced menaquinone pool, we studied NifL reduction using artificial membrane systems containing purified components of the anaerobic respiratory chain of Wolinella succinogenes. In this in vitro assay using proteoliposomes containing purified formate dehydrogenase and purified menaquinone (MK(6)) or 8-methylmenaquinone (MMK(6)) from W. succinogenes, reduction of purified NifL was achieved by formate oxidation. Furthermore, the respective reduction rates, which were determined using equal amounts of NifL, have been shown to be directly dependent on the concentration of both formate dehydrogenase and menaquinones incorporated into the proteoliposomes, demonstrating a direct electron transfer from menaquinone to NifL. When purified hydrogenase and MK(6) from W. succinogenes were inserted into the proteoliposomes, NifL was reduced with nearly the same rate by hydrogen oxidation. In both cases reduced NifL was found to be highly associated to the proteoliposomes, which is in accordance with our previous findings in vivo. On the bases of these experiments, we propose that the redox state of the menaquinone pool is the redox signal for nif regulation in K. pneumoniae by directly transferring electrons onto NifL under anaerobic conditions.
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PMID:Biochemical studies of Klebsiella pneumoniae NifL reduction using reconstituted partial anaerobic respiratory chains of Wolinella succinogenes. 1732 51

To utilize fermentative bacteria for producing the alternative fuel hydrogen, we performed successive rounds of P1 transduction from the Keio Escherichia coli K-12 library to introduce multiple, stable mutations into a single bacterium to direct the metabolic flux toward hydrogen production. E. coli cells convert glucose to various organic acids (such as succinate, pyruvate, lactate, formate, and acetate) to synthesize energy and hydrogen from formate by the formate hydrogen-lyase (FHL) system that consists of hydrogenase 3 and formate dehydrogenase-H. We altered the regulation of FHL by inactivating the repressor encoded by hycA and by overexpressing the activator encoded by fhlA, removed hydrogen uptake activity by deleting hyaB (hydrogenase 1) and hybC (hydrogenase 2), redirected glucose metabolism to formate by using the fdnG, fdoG, narG, focA, focB, poxB, and aceE mutations, and inactivated the succinate and lactate synthesis pathways by deleting frdC and ldhA, respectively. The best of the metabolically engineered strains, BW25113 hyaB hybC hycA fdoG frdC ldhA aceE, increased hydrogen production 4.6-fold from glucose and increased the hydrogen yield twofold from 0.65 to 1.3 mol H(2)/mol glucose (maximum, 2 mol H(2)/mol glucose).
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PMID:Enhanced hydrogen production from glucose by metabolically engineered Escherichia coli. 1793 9

Sulfate-reducing bacteria (SRB) are anaerobes readily found in oxic-anoxic interfaces. Multiple defense pathways against oxidative conditions were identified in these organisms and proposed to be differentially expressed under different concentrations of oxygen, contributing to their ability to survive oxic conditions. In this study, Desulfovibrio vulgaris Hildenborough cells were exposed to the highest concentration of oxygen that SRB are likely to encounter in natural habitats, and the global transcriptomic response was determined. Three hundred and seven genes were responsive, with cellular roles in energy metabolism, protein fate, cell envelope and regulatory functions, including multiple genes encoding heat shock proteins, peptidases and proteins with heat shock promoters. Of the oxygen reducing mechanisms of D. vulgaris only the periplasmic hydrogen-dependent mechanism was up-regulated, involving the [NiFeSe] hydrogenase, formate dehydrogenase(s) and the Hmc membrane complex. The oxidative defense response concentrated on damage repair by metal-free enzymes. These data, together with the down-regulation of the ferric uptake regulator operon, which restricts the availability of iron, and the lack of response of the peroxide-sensing regulator operon, suggest that a major effect of this oxygen stress is the inactivation and/or degradation of multiple metalloproteins present in D. vulgaris as a consequence of oxidative damage to their metal clusters.
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PMID:Transcriptional response of Desulfovibrio vulgaris Hildenborough to oxidative stress mimicking environmental conditions. 1806 Jun 64

DNA and RNA transcripts, particularly of genes of functional importance in the reductively dechlorinating microbe Dehalococcoides, are increasingly being studied as potential molecular bioindicators of reductive dechlorination. Ideally, mRNA bioindicators would be informative both qualitatively (with respect to dechlorination end point and substrate range) and quantitatively (with respectto activity rates). Here, we examined pseudo-steady-state mRNA levels in Dehalococcoides-containing microcosms continuously fed PCE at various loading rates. We characterized gene transcript abundance of potential Dehalococcoides bioindicators of reductive dechlorination, including 16S rRNA, and genes encoding an annotated formate dehydrogenase (Fdh), the hydrogenase (H2ase) Hup, and the reductive dehalogenases (RDases) TceA, DET1559, PceA, and DET1545. Increases in steady PCE loading rate led to corresponding increases in PCE respiration rate (1.5 +/- 0.1, 2.5 +/- 0.3, 4.8 +/- 0.1, and 9.2 +/- 0.5 micromol/L/hr). We also observed that pseudo-steady-state expression levels of most functional targets increase linearly over PCE respiration rates of 1.5-4.8 micromol/L/hr, with Fdh, Hup, and TceA transcripts increasing by approximately 2 x 10(10) copies per mL of culture for every micromol/L/hr increase in chloroethene respiration rate, and DET1559 and PceAtranscripts increasing by approximately9 x 10(9) copies per mL of culture, butthat increased respiration rates of 9.2 micromol/L/hr did not necessarily lead to corresponding increases in transcript levels.
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PMID:Correlation of respiratory gene expression levels and pseudo-steady-state PCE respiration rates in Dehalococcoides ethenogenes. 1828 40

Ruminal methane (CH(4)) production results in the loss of up to 12% of gross energy intake and contributes nearly 20% of the United States' annual emission of this greenhouse gas. We report the effects of select nitrocompounds on ruminal fermentation after 22 h in vitro incubation (39 degrees C) with or without additions of hydrogen (H(2)), formate or both. In incubations containing no added reductant, CH(4) production was inhibited 41% by 2-nitro-1-propanol (2NPOH) and >97% by 3-nitro-1-propionic acid (3NPA), nitroethane (NE) and 2-nitroethanol (2NEOH) compared to non-treated controls and H(2) did not accumulate. With formate as the sole added reductant, nitro-treatment reduced CH(4) production by >99% and caused 42% to complete inhibition of formate catabolism compared to controls, and the accumulation of H(2) increased slightly. Nitro-treatment decreased CH(4) production 57-98% from that of controls when supplied H(2) or formate plus H(2). Formate catabolism was decreased 42-84% from that in controls by all nitro-treatments except 3NPA with both formate and H(2). Greater than 97% of the added H(2) was catabolized within controls; >84% was catabolized in nitro-treated incubations. Acetate, propionate and butyrate accumulations were unaffected by nitro-treatment irregardless of reductant; however, effects on ammonia and branched chain fatty acid accumulations varied. These results suggest that nitro-treatment inhibited formate dehydrogenase/formate hydrogen lyase and hydrogenase activity.
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PMID:Effects of select nitrocompounds on in vitro ruminal fermentation during conditions of limiting or excess added reductant. 1853 64

Whole cells of Alcaligenes eutrophus (as well as isolated P. oxalaticus formate dehydrogenase and A. eutrophus hydrogenase coupled via NAD(+) or methyl viologen) have been shown to produce H(2) from formic acid. Immobilization of the cells in kappa-carrageenan gel greatly enhances their stability at room temperature. The rate of hydrogen production catalyzed by immobilized A. eutrophus has been studied as a function of the concentrations of the cells and formate and also pH. An inhibition by high concentrations of formate has been found. Immobilized cells were also capable of synthesizing formate from H(2) and bicarbonate. Yields of formate up to 30% have been obtained. The catalytic efficiency of immobilized A. eutrophus cells was compared with that of palladium adsorbed on activated carbon.
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PMID:Enzymatic synthesis of formic acid from H2 and CO2 and production of hydrogen from formic acid. 1854 98

Methanococcus maripaludis, an H(2)- and formate-utilizing methanogen, produced H(2) at high rates from formate. The rates and kinetics of H(2) production depended upon the growth conditions, and H(2) availability during growth was a major factor. Specific activities of resting cells grown with formate or H(2) were 0.4 to 1.4 U mg(-1) (dry weight). H(2) production in formate-grown cells followed Michaelis-Menten kinetics, and the concentration of formate required for half-maximal activity (K(f)) was 3.6 mM. In contrast, in H(2)-grown cells this process followed sigmoidal kinetics, and the K(f) was 9 mM. A key enzyme for formate-dependent H(2) production was formate dehydrogenase, Fdh. H(2) production and growth were severely reduced in a mutant containing a deletion of the gene encoding the Fdh1 isozyme, indicating that it was the primary Fdh. In contrast, a mutant containing a deletion of the gene encoding the Fdh2 isozyme possessed near-wild-type activities, indicating that this isozyme did not play a major role. H(2) production by a mutant containing a deletion of the coenzyme F(420)-reducing hydrogenase Fru was also severely reduced, suggesting that the major pathway of H(2) production comprised Fdh1 and Fru. Because a Deltafru-Deltafrc mutant retained 10% of the wild-type activity, an additional pathway is present. Mutants possessing deletions of the gene encoding the F(420)-dependent methylene-H(4)MTP dehydrogenase (Mtd) or the H(2)-forming methylene-H(4)MTP dehydrogenase (Hmd) also possessed reduced activity, which suggested that this second pathway was comprised of Fdh1-Mtd-Hmd. In contrast to H(2) production, the cellular rates of methanogenesis were unaffected in these mutants, which suggested that the observed H(2) production was not a direct intermediate of methanogenesis. In conclusion, high rates of formate-dependent H(2) production demonstrated the potential of M. maripaludis for the microbial production of H(2) from formate.
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PMID:Formate-dependent H2 production by the mesophilic methanogen Methanococcus maripaludis. 1879 Oct 18

The effect of tungsten (W) and molybdenum (Mo) on the growth of Syntrophobacter fumaroxidans and Methanospirillum hungatei was studied in syntrophic cultures and the pure cultures of both the organisms. Cells that were grown syntropically were separated by Percoll density centrifugation. Measurement of hydrogenase and formate dehydrogenase levels in cell extracts of syntrophically grown cells correlated with the methane formation rates in the co-cultures. The effect of W and Mo on the activity of formate dehydrogenase was considerable in both the organisms, whereas hydrogenase activity remained relatively constant. Depletion of tungsten and/or molybdenum, however, did not affect the growth of the pure culture of S. fumaroxidans on propionate plus fumarate significantly, although the specific activities of hydrogenase and especially formate dehydrogenase were influenced by the absence of Mo and W. This indicates that the organism has a low W or Mo requirement under these conditions. Growth of M. hungatei on either formate or H2/CO2 required tungsten, and molybdenum could replace tungsten to some extent. Our results suggest a more prominent role for H2 as electron carrier in the syntrophic conversion of propionate, when the essential trace metals W and Mo for the functioning of formate dehydrogenase are depleted.
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PMID:Effect of tungsten and molybdenum on growth of a syntrophic coculture of Syntrophobacter fumaroxidans and Methanospirillum hungatei. 1879 63

The human pathogen Campylobacter jejuni utilizes oxidative phosphorylation to meet all of its energy demands. The genome sequence of this bacterium encodes a number of respiratory enzymes in a branched electron transport chain that predicts the utilization of a number of electron transport chain donor and acceptor molecules. Three of these electron donor enzymes: hydrogenase, formate dehydrogenase, and 2-oxoglutarate:acceptor oxidoreductase (OOR), oxidize hydrogen, formate and alpha-ketoglutarate as electron donors, respectively. Mutations were created in these donor enzymes to isolate mutants in hydrogenase (HydB::CM), formate dehydrogenase (Fdh::CM), and OOR (OorB::CM), as well as a strain with insertions in both hydrogenase and formate dehydrogenase (Hyd::Fdh). These mutants are deficient in their respective enzyme activities and do not reduce the components of the electron transport chain when provided with their respective substrates. The presence of either hydrogen or formate in the media stimulated the growth of wild type (WT) C. jejuni (but not the associated mutant strains) and at least one of these alternative substrates is required for growth of the OOR mutant strain OorB::CM. Finally, the importance of hydrogenase, formate dehydrogenase and OOR as well as the complex I of C. jejuni are elucidated by chicken colonization assays, where the double mutant Hyd::Fdh, OorB::CM and nuo mutants are severely impaired in host colonization.
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PMID:The role of respiratory donor enzymes in Campylobacter jejuni host colonization and physiology. 1939 93

End-product synthesis and enzyme activities involved in pyruvate catabolism, H(2) synthesis, and ethanol production in mid-log (OD(600) approximately 0.25), early stationary (OD(600) approximately 0.5), and stationary phase (OD(600) approximately 0.7) cell extracts were determined in Clostridium thermocellum ATCC 27405 grown in batch cultures on cellobiose. Carbon dioxide, hydrogen, ethanol, acetate and formate were major end-products and their production paralleled growth and cellobiose consumption. Lactate dehydrogenase, pyruvate:formate lyase, pyruvate:ferredoxin oxidoreductase, methyl viologen-dependant hydrogenase, ferredoxin-dependant hydrogenase, NADH-dependant hydrogenase, NADPH-dependant hydrogenase, NADH-dependant acetaldehyde dehydrogenase, NADH-dependant alcohol dehydogenase, and NADPH-dependant alcohol dehydrogenase activities were detected in all extracts, while pyruate dehydrogenase and formate dehydrogenase activities were not detected. All hydrogenase activities decreased (2-12-fold) as growth progressed from early exponential to stationary phase. Alcohol dehydrogenase activities fluctuated only marginally (<45%), while lactate dehydrogenase, pyruvate:formate lyase, and pyruvate:ferredoxin oxidoreductase remained constant in all cell extracts. We have proposed a pathway involved in pyruvate catabolism and end-product formation based on enzyme activity profiles in conjunction with bioinformatics analysis.
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PMID:Growth phase-dependant enzyme profile of pyruvate catabolism and end-product formation in Clostridium thermocellum ATCC 27405. 1942 11


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