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)

A newly observed general chlorophyll fluorescence induction effect in plants is described. Fluorescence yield can rise through as many as four different phases (alpha, beta, gamma, ) in the dark, when intact cells or leaves are rapidly heated (within approx. 2.5 s) from 20 to 40-50 degrees C. An analysis of this temperature-jump fluorescence induction in Scenedesmus obliquus leads to the following: 1. Phase alpha is due to removal of S-quenching and appears to be related to heat deactivation of the water-splitting enzyme system. With prolonged heating, irreversibility of alpha upon recooling reflects irreversible damage to the water-splitting enzyme system. 2. beta is independent of the S-states and of the redox state of primary System II acceptor Q. It is suggested that beta parallels functional separation of Q from the System II trapping centre. This effect is highly reversible. 3. gamma and beta reflect reduction of primary System II acceptor Q by a heat-induced endogenous reductant, which is probably identical to hydrogenase. Critical temperatures for pronounced alpha and beta phases differ markedly in different plants. Possible correlations between temperature-jump fluorescence inductio, thylakoid membrane lipid composition, lipid phase transition and lipid-protein interactions are discussed.
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PMID:Analysis of temperature-jump chlorophyll fluorescence induction in plants. 124 10

The pH values in reversed micelles were measured, making use of the hydrogenase enzyme as redox catalyst short-circuiting the viologen oxidized/semiquinone redox states. The hydrogenases from Desulfovibrio vulgaris (Hildenborough) and from Megasphaera elsdenii were applied. The observed pH values in reversed micelles were not dependent on the type of hydrogenase. Two cationic [cetyltrimethylammonium bromide and dodecylammonium propionate (DAP)] and two anionic sodiumdodecyl sulphate, sodium di(ethylhexyl)sulfosuccinate types of reversed micelles were used in combination with viologens having distinguishable valencies. It was observed that, in the cationic-reversed micelles, the dissociation constant for the semiquinone dimer had about the same value as compared to bulk water, while this value was significantly higher in the anionic-reversed micelles. Furthermore, the dissociation constant was independent of the concentration of viologen semiquinone in the reversed micelle, indicating that exchange kinetics are faster than the dimerisation process. With the exception of DAP, a linear relation exists, pH = a.pHrm + b, between the pH of the bulk water and the pH as measured in the reversed micelle (pHrm). In all these cases the value of a is smaller than unity, the value of b ranges between 1.6-2.7. For DAP the pHrm is always around 7. In DAP-reversed micelles, the counter-ion propionate probably serves as an internal buffer. Using cytochrome c3 as pH indicator in combination with N,N'-di(3-aminopropyl)-4,4'-bipyridinium)4+ to take care of electron transfer, in cetyltrimethylammonium-bromide-reversed micelles the pHrm is about the same as indicated by the viologen; in SDS-reversed micelles the pHrm is always lower than that indicated by N,N'-di(3-aminopropyl)4,4'-pyridinium4+. In contrast to cytochrome c3 from D. vulgaris, which in reversed micelles cannot become reduced directly by its D. vulgaris hydrogenase, the hydrogenase of M. elsdenii is able to reduce its ferredoxin directly.
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PMID:The pH in reversed micelles as imposed by the dihydrogen/proton redox couple and indicated by viologens and cytochrome c3 using hydrogenase as redox catalyst. 132 16

Bovine mitochondrial NADH-ubiquinone reductase (complex I), the first enzyme in the electron-transport chain, is a membrane-bound assembly of more than 30 different proteins, and the flavoprotein (FP) fraction, a water-soluble assembly of the 51-, 24-, and 10-kDa subunits, retains some of the catalytic properties of the enzyme. The 51-kDa subunit binds the substrate NAD(H) and probably contains both the cofactor, FMN, and also a tetranuclear iron-sulfur center, while a binuclear iron-sulfur center is located in the 24- or 10-kDa proteins. The 75-kDa subunit is the largest of the six proteins in the iron-sulfur protein (IP) fraction, and its sequence indicates that it too contains iron-sulfur clusters. Partial protein sequences have been determined at the N-terminus and at internal sites in the 51-kDa subunit, and the corresponding cDNA encoding a precursor of the protein has been isolated by using a novel strategy based on the polymerase chain reaction. The mature protein is 444 amino acids long. Its sequence, and those of the 24- and 75-kDa subunits, shows that mitochondrial complex I is related to a soluble NAD-reducing hydrogenase from the facultative chemolithotroph Alcaligenes eutrophus H16. This enzyme has four subunits, alpha, beta, gamma, and delta, and the alpha gamma dimer is an NADH oxidoreductase that contains FMN. The gamma-subunit is related to residues 1-240 of the 75-kDa subunit of complex I, and the alpha-subunit sequence is a fusion of homologues of the 24- and 51-kDa subunits, in the order N- to C-terminal. The most highly conserved regions are in the 51-kDa subunit and probably form parts of nucleotide binding sites for NAD(H) and FMN. Another conserved region surrounds the sequence motif CysXXCysXXCys, which is likely to provide three of the four ligands of a 4Fe-4S center, possibly that known as N-3. Characteristic ligands for a second 4Fe-4S center are conserved in the 75-kDa and gamma-subunits. This relationship with the bacterial enzyme implies that the 24- and 51-kDa subunits, together with part of the 75-kDa subunit, constitute a structural unit in mitochondrial complex I that is concerned with the first steps of electron transport.
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PMID:Relationship between mitochondrial NADH-ubiquinone reductase and a bacterial NAD-reducing hydrogenase. 190 Jan 94

Bacillus cereus strain Socransky 67 and Streptococcus mutans strain Ingbritt were grown overnight in complex medium and then in fresh medium flasks for 5 h. The bacterial cells in the medium were centrifuged and resuspended; 4-14C-progesterone or 4-14C-testosterone was added, and the samples were incubated for 2 h at 37 degrees C in a shaking water bath. The metabolites were analyzed with column and thin layer chromatography and radioautography and quantified by liquid scintillation counting. On the basis of the metabolites found it was concluded that B. cereus strain Socransky 67 contains 5 alpha-steroid hydrogenase, and 3 beta-, 17 beta- and 20 alpha-hydroxysteroid dehydrogenases and probably also steroid hydroxylases, and that S. mutans strain Ingbritt contains 5 alpha- and 5 beta-steroid hydrogenases, and 3 alpha-, 17 beta- and 20 alpha-hydroxysteroid dehydrogenases. The metabolic activity of B. cereus is several times higher than that of S. mutans. We suggest that the greater ability of B. cereus to metabolize progesterone and testosterone is probably due to its growth milieu in the gingival sulcus, where it is nearer to the gingival tissue.
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PMID:Metabolism of progesterone and testosterone by Bacillus cereus strain Socransky 67 and Streptococcus mutans strain Ingbritt. 212 57

An original gas chromatographic-mass spectrometric technique is described for studying simultaneous dihydrogen-deuteron exchange and para-ortho H2 conversion catalyzed by different Desulfovibrio hydrogenases. Para and orthohydrogens are separated on an alumina column at the temperature of liquid nitrogen, but if both HD and ortho H2 are present, their retention times are too close to each other for total separation and only one peak is observed with a thermal conductivity detector. In order to resolve the peaks from one another, a fraction of the gas released from the gas chromatograph column is admitted to the ion source of a mass spectrometer, where the gases are separated according to their respective masses. Because of a peak-jumping system, the different components involved in the exchange and in the conversion reactions can be scanned so that the spectra corresponding to mass m/e 2 (para and ortho H2), m/e 3 (HD), and m/e 4 (D2) can be obtained simultaneously. This technique has been employed to resolve a controversial problem concerning the occurrence or lack of any para-orthohydrogen conversion in heavy water. Actually both exchange and conversion were demonstrated to occur with a (NiFe) hydrogenase, whereas with a (NiFeSe) hydrogenase, which had an exchange activity equivalent to that of the former, practically no para-ortho conversion could be observed in D2O. These findings are related to the constitutional and catalytic properties of the hydrogenases belonging to the different classes.
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PMID:A gas chromatographic-mass spectrometric technique for studying simultaneous hydrogen-deuteron exchange and para-orthohydrogen conversion in hydrogenases of Desulfovibrio vulgaris Hildenborough. 222 93

The nickel centre of hydrogenase from Desulfovibrio gigas was studied by electron spin echo envelope modulation (ESEEM) spectroscopy in the oxidized, unready (Ni-A) and H2-reduced active (Ni-C) states, both in H2O and 2H2O solutions. Fourier transforms of the 3-pulse ESEEM, taken at 8.7 GHz, for Ni-A and Ni-C in H2O contained similar peaks with narrow linewidths at frequencies of 0.4, 1.2 and 1.6 MHz, and a broader peak centered at 4.5 MHz. At 11.6 GHz, the low frequency components showed small field-dependent shifts, while the high frequency component was shifted to 5.1 MHz. These results are consistent with the presence of 14N, possibly from imidazole, coupled to the nickel centre. In 2H2O, Ni-A was shown to be inaccessible for exchange with solvent deuterons. In contrast, Ni-C was accessible to solvent exchange, with a deuterium population being in close proximity to the metal ion. Thus, the nickel environment of the active protein is different from that in the oxidized or unready state. On illumination of Ni-C, although EPR changes are seen, 14N coupling remains, and for the 2H2O sample, deuterium coupling is also retained.
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PMID:A pulsed EPR study of redox-dependent hyperfine interactions for the nickel centre of Desulfovibrio gigas hydrogenase. 284 56

Redox titrations with hydrogenase from Chromatium vinosum show that its nickel ion can exist in 3, possibly 4, different redox states: the 3+, 2+, 1+ and possibly a zero valent state. The 1+ state is unstable: oxidation to Ni(II) occurs unless H2 gas is present. The Ni(I) coordination, but not that of Ni(III), is highly light sensitive. A photoreaction occurs on illumination. It is irreversible below 77 K, but reversible at 200 K. The rate of this photodissociation reaction in 2H2O is nearly 6-times slower than in H2O, indicating the breakage of a nickel-hydrogen bond. This forms the first evidence for an H atom in the direct coordination sphere of Ni in hydrogenase and for the involvement of this metal in the reaction with hydrogen.
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PMID:Monovalent nickel in hydrogenase from Chromatium vinosum. Light sensitivity and evidence for direct interaction with hydrogen. 298 5

Evidence will be presented in this review article that the application of hydrogenase has large biotechnological possibilities. Our investigations show: Fast reaction of hydrogenase at an electrode surface to reduce H+; Photochemical production of H2 by hydrogenase by photosensitized Ru-complexes dissolved in reversed micellar membranes and vectorial H+ transport through the membrane to the water phase; The production of fine chemicals in reversed micelles by a system containing specific enzymes, hydrogenase and H2. The rules to obtain maximal conversion rates with this system will be presented.
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PMID:Application of hydrogenase in biotechnological conversions. 301 46

From the numerous possibilities of biological solar energy transduction the production of hydrogen was selected in our laboratory. There are two forms of H2 production: from biomass with enzymes (formate-hydrogen lyase and hydrogenase enzymes) and the exploitation of some living systems or their analogs to evolve H2 from water upon solar irradiation. To approach the first problem, a bacterial strain and a hydrogenase (H2ase) enzyme of good parameters were isolated. The system composed produced H2 from biomass with an energetic efficiency of 10-12 per cent. Dealing with the second task, by changing some environmental factors we succeeded to increase by a factor of 15 the quantity of H2 produced by Anabeana cylindrica from water in light. It is clear from these studies that further research is needed to understand better the mechanism and regulation of biological H2 production. The aim of this research is to utilize it as an economically feasible and environmentally harmless energy source.
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PMID:Possibilities of biological energy production. 309 12

Soybean nodule bacteroids and Bradyrhizobium japonicum free-living cells induced for H2-uptake hydrogenase, actively catalyze the evolution of H2 in a reaction highly dependent on the pH. The optimal pHs for the evolution and uptake reactions were 4.0 and 7.5-8.0, respectively. No differences were found between free-living cells and bacteroids with respect to hydrogen acceptor specificity, although absolute rates of H2 uptake were higher for free-living cells. Both types of cells were able to evolve hydrogen from reduced methyl viologen at low pH. These intact cells also catalyzed the exchange reaction between tritium and water in the absence of oxygen. The pH profile of the exchange activity showed two peaks at values near the optimal pHs for the evolution and uptake reactions.
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PMID:Effect of pH on tritium exchange and hydrogen production and uptake in free-living cells and in bacteroids of Bradyrhizobium japonicum. 332 98


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