Oxidation Of Molecular Hydrogen Research Articles

Autotrophic growth of Acidithiobacillus ferrooxidans by oxidation of molecular hydrogen using a gas–liquid contactor

The iron-oxidizing bacterium, Acidithiobacillus ferrooxidans, was cultivated on a medium without ferrous iron. Molecular hydrogen and air were supplied to the medium. It was found that A. ferrooxidans could grow with hydrogen in the pH range between 2.0 and 3.5. A trickle-bed contactor was used to increase the dissolution rate of hydrogen. The doubling time was increased and the cell concentration reached 4.0 × 10 9 cells ml −1 after 6 days. When the cells taken from the hydrogen medium were transferred back into the medium containing ferrous iron, the growth rate and the iron-oxidizing ability were the same as the predictions assuming that the microorganism grown with hydrogen was A. ferrooxidans.

Remediation of TCE-contaminated groundwater using zero valent iron and direct current: experimental results and electron competition model

The objectives of this study are to design an optimal electro-enhanced permeable reactive barrier (E2PRB) system for the remediation of trichloroethylene (TCE)-contaminated water using zero valent iron (ZVI) and direct current (DC) and to investigate the mechanisms responsible for TCE degradation in different ZVI-DC configurations. A series of column experiments was conducted to evaluate the effect of different arrangements of electrodes and ZVI barriers in the column on the TCE removal capacity (RC). In twelve different combinations of ZVI and/or DC application in the test columns, the rate of reductive dechlorination of TCE was improved up to six times with simultaneous application of ZVI and DC compared to that using ZVI only. The most effective arrangement of electrode and ZVI for TCE removal was the column set with ZVI and a cathode installed at the down gradient. Based on the electrokinetic study for the column systems with only DC input, single acid front movement could explain different RCs. An enhanced dechlorination rate of TCE using E2PRB systems, compared to a conventional PRB system, was observed, and is considered to be attributed to more electron sources: (1) external DC, (2) electrolysis of water, (3) oxidation of ZVI, (4) oxidation of dissolved Fe2+, (5) oxidation of molecular hydrogen at the cathode, and (6) oxidation of Fe2+ in mineral precipitates. Each of these electron sources was evaluated for their potential influencing the TCE RC through the electron competition model and energy consumption. A strong correlation between the quantity of electrons generated, RC, and the energy-effectiveness was found.

Dithiolato-Bridged Dinuclear Iron−Nickel Complexes [Fe(CO)2(CN)2(μ-SCH2CH2CH2S)Ni(S2CNR2)]-Modeling the Active Site of [NiFe] Hydrogenase

[NiFe] hydrogenase, the enzyme of which catalyzes the reversible oxidation of molecular hydrogen to protons and electrons, contains a unique heterodinuclear thiolate-bridged Ni-Fe complex in which the iron center is coordinated by CO and CN. We have synthesized dithiolate-bridged Ni-Fe complexes bearing CO and CN ligands to model the active center of [NiFe] hydrogenase. The Ni-Fe complexes containing a [(CN)2(CO)2Fe(mu-S2)NiS2] framework are the closest yet structural models of [NiFe] hydrogenase.

Hydrogen and bioenergetics in the Yellowstone geothermal ecosystem

The geochemical energy budgets for high-temperature microbial ecosystems such as occur at Yellowstone National Park have been unclear. To address the relative contributions of different geochemistries to the energy demands of these ecosystems, we draw together three lines of inference. We studied the phylogenetic compositions of high-temperature (>70 degrees C) communities in Yellowstone hot springs with distinct chemistries, conducted parallel chemical analyses, and carried out thermodynamic modeling. Results of extensive molecular analyses, taken with previous results, show that most microbial biomass in these systems, as reflected by rRNA gene abundance, is comprised of organisms of the kinds that derive energy for primary productivity from the oxidation of molecular hydrogen, H2. The apparent dominance by H2-metabolizing organisms indicates that H2 is the main source of energy for primary production in the Yellowstone high-temperature ecosystem. Hydrogen concentrations in the hot springs were measured and found to range up to >300 nM, consistent with this hypothesis. Thermodynamic modeling with environmental concentrations of potential energy sources also is consistent with the proposed microaerophilic, hydrogen-based energy economy for this geothermal ecosystem, even in the presence of high concentrations of sulfide.

Plasma supported combustion

Oxidation of molecular hydrogen and different hydrocarbons in stoichiometric mixtures with air and oxygen in the pulsed nanosecond discharges was studied at room temperature, and the detailed kinetics of the process has been numerically investigated. In the discharge afterglow, the reactions including electron-excited particles play a dominant role for the time up to 100 ns, ion–molecular reactions—for the time of microsecond range, and reactions including radicals mostly contribute for the time interval of several milliseconds. The principal role of processes with formation of excited components that support the development of the chain mechanism of oxidation has been shown. The spatial uniformity of the gas-mixture combustion initiated by a high-voltage nanosecond volume discharge is investigated at gas pressures of 0.3–2.4 atm and temperatures of 1000–2250 K. The self-ignition time and the time of discharge-induced ignition are determined. It is found that the discharge significantly (by 600 K) decreases the ignition temperature with very low energy in the discharge (∼10 −2 J/cm 3). The influence of gas excitation by a pulsed nanosecond discharge with a high-voltage pulse amplitude up to 25 kV on the properties of a premixed propane–air flame has been investigated over a wide range of the equivalence ratios (0.4–5). It was experimentally found that the flame’s blow-off velocity increased more than twice at a discharge energy input less than 1% of the burner power. Efficient production of active radicals under the action of a barrier discharge has been observed. The increase in the flame’s propagation velocity is explained by the production of atomic oxygen in a discharge by the quenching of electronically excited molecular nitrogen N 2 and the dissociation of molecular oxygen on electron-impact. A numerical model has been developed, which describes the influence of pulsed electric discharges on the ignition, combustion, and flame propagation.

New directions in gold catalysis

In the last decade there has been an explosion in the interest shown in catalysis by gold. It is now recognised that gold has unique properties as a catalyst for many reactions with pre-eminence in heterogeneous catalytic oxidation. This paper sets out the general content of a keynote lecture delivered at the second world congress on gold in Vancouver in 2003. The background to this significant interest is discussed and the early work in the field is placed in context. The current areas of interest are described and two reactions, namely the oxidation of glycerol to glyceric acid and the formation of hydrogen peroxide from the oxidation of molecular hydrogen, are discussed. The prospects for future discoveries are also considered.

Fe-only hydrogenases: structure, function and evolution

Hydrogenases are enzymes capable of catalyzing the oxidation of molecular hydrogen or its production from protons and electrons according to the reversible reaction: H2⇌2H++2e−. Most of these enzymes fall into to major classes: NiFe and Fe-only hydrogenases. Extensive spectroscopic, electrochemical and structural studies have shed appreciable light on the catalytic mechanism of hydrogenases. Although evolutionarily unrelated, NiFe and Fe-hydrogenases share a common, unusual feature: an active site low-spin Fe center with CO and CN coordination. We have recently focused our attention on Fe-hydrogenases because from structural studies by us and others, it appears to be a simpler system than the NiFe counterpart. Thus the primary hydrogen binding site has been identified and plausible, electron, proton and hydrogen pathways from and to the buried active site may be proposed from the structural data. The extensive genome sequencing effort currently under way has shown that eukaryotic organisms contain putatively gene coding sequences that display significant homology to Fe-hydrogenases. Here, we summarize the available evidence concerning the mechanism of these enzymes and carry out a structural comparison between Fe-hydrogenases and related proteins of unknown metal content from yeast, plant, worm, insect and mammals.

Conformational component in the coupled transfer of multiple electrons and protons in a monomeric tetraheme cytochrome.

Cell metabolism relies on energy transduction usually performed by complex membrane-spanning proteins that couple different chemical processes, e.g. electron and proton transfer in proton-pumps. There is great interest in determining at the molecular level the structural details that control these energy transduction events, particularly those involving multiple electrons and protons, because tight control is required to avoid the production of dangerous reactive intermediates. Tetraheme cytochrome c(3) is a small soluble and monomeric protein that performs a central step in the bioenergetic metabolism of sulfate reducing bacteria, termed "proton-thrusting," linking the oxidation of molecular hydrogen with the reduction of sulfate. The mechano-chemical coupling involved in the transfer of multiple electrons and protons in cytochrome c(3) from Desulfovibrio desulfuricans ATCC 27774 is described using results derived from the microscopic thermodynamic characterization of the redox and acid-base centers involved, crystallographic studies in the oxidized and reduced states of the cytochrome, and theoretical studies of the redox and acid-base transitions. This proton-assisted two-electron step involves very small, localized structural changes that are sufficient to generate the complex network of functional cooperativities leading to energy transduction, while using molecular mechanisms distinct from those established for other Desulfovibrio sp. cytochromes from the same structural family.

Classification and phylogeny of hydrogenases.

Hydrogenases (H2ases) catalyze the reversible oxidation of molecular hydrogen and play a central role in microbial energy metabolism. Most of these enzymes are found in Archaea and Bacteria, but a few are present in Eucarya as well. They can be distributed into three classes: the [Fe]-H2ases, the [NiFe]-H2ases, and the metal-free H2ases. The vast majority of known H2ases belong to the first two classes, and over 100 of these enzymes have been characterized genetically and/or biochemically. Compelling evidence from sequences and structures indicates that the [NiFe]- and [Fe]-H2ases are phylogenetically distinct classes of proteins. The catalytic core of the [NiFe]-H2ases is a heterodimeric protein, although additional subunits are present in many of these enzymes. Functional classes of [NiFe]-H2ases have been defined, and they are consistent with categories defined by sequence similarity of the catalytic subunits. The catalytic core of the [Fe]-H2ases is a ca. 350-residue domain that accommodates the active site (H-cluster). A few monomeric [Fe]-H2ases are barely larger than the H-cluster domain. Many others are monomeric as well, but possess additional domains that contain redox centers, mostly iron-sulfur. Some [Fe]-H2ases are oligomeric. The modular structure of H2ases is strikingly illustrated in recently unveiled sequences and structures. It is also remarkable that most of the accessory domains and subunits of H2ases have counterparts in other redox complexes, in particular NADH-ubiquinone oxidoreductase (Complex I) of respiratory chains. Microbial genome sequences are bringing forth a significant body of additional H2ase sequence data and contribute to the understanding of H2ase distribution and evolution. Altogether, the available data suggest that [Fe]-H2ases are restricted to Bacteria and Eucarya, while [NiFe]-H2ases, with one possible exception, seem to be present only in Archaea and Bacteria. H2ase processing and maturation involve the products of several genes which have been identified and are currently being characterized in the case of the [NiFe]-H2ases. In contrast, near to nothing is known regarding the maturation of the [Fe]-H2ases. Inspection of the currently available genome sequences suggests that the [NiFe]-H2ase maturation proteins have no similar counterparts in the genomes of organisms possessing [Fe]-H2ases only. This observation, if confirmed, would be consistent with the phylogenetic distinctiveness of the two classes of H2ases. Sequence alignments of catalytic subunits of H2ases have been implemented to construct phylogenetic trees that were found to be consistent, in the main, with trees derived from other data. On the basis of the comparisons performed and discussed here, proposals are made to simplify and rationalize the nomenclature of H2ase-encoding genes.

Hydrogen oxidation in a stoichiometric hydrogen-air mixture in the fast ionization wave

Oxidation of molecular hydrogen in a stoichiometric hydrogen-air mixture in the fast ionization wave (FIW) was studied at total pressures p = 1–8 Torr, and the detailed kinetics of the process has been numerically investigated. The excitation of the gas in FIW and the dynamics of molecular hydrogen concentration were monitored using measurements of absolute H2 radiation intensity (transition a 3Σ+ g → b 3Σ+ u). A comparison of calculated and experiment results allows one to draw the conclusion that the gas is predominantly excited behind the FIW front in relatively low electric fields E/n ≃ 300–600 Td at electron concentration n e ≃ (1–2) × 1012 cm−3 for a time of the order of 10 ns and can be described with good accuracy using the two-term approximation of Boltzmann's equation. In the following processes the reactions including electron-excited particles play a dominant role for times up to 100 ns, ion-molecular reactions - for the microsecond time range, reactions including radicals mostly contribute for time intervals of several milliseconds. The most critical processes have been separated for each time interval. The principal role of processes with formation of excited components that support the development of the chain mechanism of oxidation have been shown.

Construction of multicomponent catalytic films based on avidin-biotin technology for the electroenzymatic oxidation of molecular hydrogen

Two methods based on the avidin-biotin technology were developed for the multimonolayer immobilization of Desulfovibrio gigas hydrogenase on glassy carbon or gold electrodes. In both methods the molecular structure of the modified interface was the result of a step-by-step process. The first method alternates monolayers of avidin and biotinylated hydrogenase, the mediator (methyl viologen) being free to diffuse in the structure. In the second method, the avidin monolayers were used to immobilize both the biotinylated enzyme and a long-chain biotinylated viologen derivative. The viologen head of this hydrophilic arm shuttles the electrons between the electrode and the enzyme. The modified electrodes were evaluated for the electroenzymatic oxidation of molecular hydrogen, which has interest for the development of enzymatic fuel cells. The parameters that affect the current density of mediated oxidation of H2 at the modified electrodes was studied. The second structure, which has given typical catalytic currents of 25 μA per cm2 for 10 monolayers, was found clearly less efficient than the first structure (500 μA per cm2 for 10 monolayers). In both methods the catalytic currents increased linearly with the number of monolayers of hydrogenase immobilized, which indicates that the multilayer structures are spatially ordered. © 2000 John Wiley & Sons, Inc. Biotechnol Bioeng 68: 1–10, 2000.

Construction of multicomponent catalytic films based on avidin-biotin technology for the electroenzymatic oxidation of molecular hydrogen.

Two methods based on the avidin-biotin technology were developed for the multimonolayer immobilization of Desulfovibrio gigas hydrogenase on glassy carbon or gold electrodes. In both methods the molecular structure of the modified interface was the result of a step-by-step process. The first method alternates monolayers of avidin and biotinylated hydrogenase, the mediator (methyl viologen) being free to diffuse in the structure. In the second method, the avidin monolayers were used to immobilize both the biotinylated enzyme and a long-chain biotinylated viologen derivative. The viologen head of this hydrophilic arm shuttles the electrons between the electrode and the enzyme. The modified electrodes were evaluated for the electroenzymatic oxidation of molecular hydrogen, which has interest for the development of enzymatic fuel cells. The parameters that affect the current density of mediated oxidation of H(2) at the modified electrodes was studied. The second structure, which has given typical catalytic currents of 25 microA per cm(2) for 10 monolayers, was found clearly less efficient than the first structure (500 microA per cm(2) for 10 monolayers). In both methods the catalytic currents increased linearly with the number of monolayers of hydrogenase immobilized, which indicates that the multilayer structures are spatially ordered.

Respiration of 2,4,6-trinitrotoluene by Pseudomonas sp. strain JLR11.

Under anoxic conditions Pseudomonas sp. strain JLR11 can use 2,4, 6-trinitrotoluene (TNT) as the sole N source, releasing nitrite from the aromatic ring and subsequently reducing it to ammonium and incorporating it into C skeletons. This study shows that TNT can also be used as a terminal electron acceptor in respiratory chains under anoxic conditions by Pseudomonas sp. strain JLR11. TNT-dependent proton translocation coupled to the reduction of TNT to aminonitrotoluenes has been observed in TNT-grown cells. This extrusion did not occur in nitrate-grown cells or in anaerobic TNT-grown cells treated with cyanide, a respiratory chain inhibitor. We have shown that in a membrane fraction prepared from Pseudomonas sp. strain JLR11 grown on TNT under anaerobic conditions, the synthesis of ATP was coupled to the oxidation of molecular hydrogen and to the reduction of TNT. This phosphorylation was uncoupled by gramicidin. Respiration by Pseudomonas sp. strain JLR11 is potentially useful for the biotreatment of TNT in polluted waters and soils, particularly in phytorhizoremediation, in which bacterial cells are transported to the deepest root zones, which are poor in oxygen.

A sequential electron transfer from hydrogenases to cytochromes in sulfate-reducing bacteria

A central step in the energy metabolism of sulfate-reducing bacteria is the oxidation of molecular hydrogen, catalyzed by a periplasmic hydrogenase. The resulting electrons are then transferred to various electron transport chains and used for cytoplasmic sulfate reduction. The complex formation between [NiFeSe] hydrogenase and the soluble periplasmic polyheme cytochromes from Desulfomicrobium norvegicum was characterized by cross-linking experiments, BIAcore and kinetics analysis. Analysis of electron transfer between [NiFeSe] hydrogenase and octaheme cytochrome c 3 ( M r 26 000) pointed out that this cytochrome is reduced faster in the presence of catalytic amounts of tetraheme cytochrome c 3 ( M r 13 000) isolated from the same organism. The activation of the hydrogenase-dependent reduction of polyheme cytochromes by cytochrome c 3 ( M r 13 000), which is now described in both Desulfovibrio and Desulfomicrobium, is proposed as a general mechanism. During this process, cytochrome c 3 ( M r 13 000) would act as an electron shuttle in between hydrogenase and the polyheme cytochromes and its conductivity appears to be an important factor.

A novel multicomponent regulatory system mediates H2 sensing in Alcaligenes eutrophus.

Oxidation of molecular hydrogen catalyzed by [NiFe] hydrogenases is a widespread mechanism of energy generation among prokaryotes. Biosynthesis of the H2-oxidizing enzymes is a complex process subject to positive control by H2 and negative control by organic energy sources. In this report we describe a novel signal transduction system regulating hydrogenase gene (hox) expression in the proteobacterium Alcaligenes eutrophus. This multicomponent system consists of the proteins HoxB, HoxC, HoxJ*, and HoxA. HoxB and HoxC share characteristic features of dimeric [NiFe] hydrogenases and form the putative H2 receptor that interacts directly or indirectly with the histidine protein kinase HoxJ*. A single amino acid substitution (HoxJ*G422S) in a conserved C-terminal glycine-rich motif of HoxJ* resulted in a loss of H2-dependent signal transduction and a concomitant block in autophosphorylating activity, suggesting that autokinase activity is essential for the response to H2. Whereas deletions in hoxB or hoxC abolished hydrogenase synthesis almost completely, the autokinase-deficient strain maintained high-level hox gene expression, indicating that the active sensor kinase exerts a negative effect on hox gene expression in the absence of H2. Substitutions of the conserved phosphoryl acceptor residue Asp55 in the response regulator HoxA (HoxAD55E and HoxAD55N) disrupted the H2 signal-transduction chain. Unlike other NtrC-like regulators, the altered HoxA proteins still allowed high-level transcriptional activation. The data presented here suggest a model in which the nonphosphorylated form of HoxA stimulates transcription in concert with a yet unknown global energy-responsive factor.

Redox-Bohr effect in electron/proton energy transduction: cytochrome c 3 coupled to hydrogenase works as a 'proton thruster' in Desulfovibrio vulgaris

A central step in the metabolism of Desulfovibrio spp. is the oxidation of molecular hydrogen catalyzed by a periplasmic hydrogenase. However, this enzymatic activity is quite low at physiological pH. The hypothesis that, in the presence of the tetrahaem cytochrome c 3, hydrogenase can maintain full activity at physiological pH through the concerted capture of the resulting electrons and protons by the cytochrome was tested for the case of Desulfovibrio vulgaris (Hildenborough). The crucial step involves an electron-to-proton energy transduction, and is achieved through a network of cooperativities between redox and ionizable centers within the cytochrome (redox-Bohr effect). This mechanism, which requires a relocation of the proposed proton channel in the hydrogenase structure, is similar to that proposed for the transmembrane proton pumps, and is the first example which shows evidence of functional energy transduction in the absence of a membrane confinement.

Anodically grown porous silicon structure: formation mechanisms

It is experimentally shown, in porous silicon formation, that there is an increase in dissolution rate at fluorine-covered sites of the silicon surface due to the presence of excess electrons coming from the oxidation of molecular hydrogen at hydrogen-covered sites. The increase in dissolution rate in the presence of excess charge at the fluorine-covered sites is investigated theoretically by a semi-empirical Hartree-Fock calculation which shows that this spatially variable dissolution generates the porous silicon structure.

Spatially variable reaction in the formation of anodically grown porous silicon structures

In porous silicon formations there is an increase of dissolution rate at the fluorine-covered sites of the silicon surface due to the presence of excess electrons coming from oxidation of molecular hydrogen at the passivated (hydrogen-covered) sites. The dissolution rate increase in the presence of excess charge at the fluorine-covered sites is experimentally measured and a theoretical investigation is carried out by a semiempirical Hartree–Fock calculation. This spatially variable dissolution generates the porous silicon surface.

Energetics of molecular hydrogen oxidation in the oral pathogen Campylobacter rectus.

Energetics of molecular hydrogen oxidation in the oral pathogen Campylobacter rectus.

Electrocatalytic reduction of nitric acid at rhodized electrodes and its inhibition by chloride ions

The electrocatalytic reduction of nitric acid was studied at rhodized electrodes with low (10–25) roughness factor values in 1 mol dm −3 H 2SO 4 supporting electrolyte. A simple logarithmic current vs. potential relationship was found for the cases where the role of transport processes could be neglected. Consequently, a simple charge transfer reaction could be considered as rate determining step. The inhibition of the reduction process by the adsorption of chloride ions was studied and it was shown that the potential and concentration dependent adsorption of Cl − species triggers potential oscillations under galvanostatic conditions. Similar oscillatory behaviour was observed under open circuit conditions in a hydrogen atmosphere, ie the oscillation of the mixed potential of two coupled reactions, the reduction of nitrate and oxidation of molecular hydrogen, takes place.