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31.
Chromosomal mutants of Alcaligenes eutrophus unable to grow with molecular hydrogen as the energy source also failed to grow with nitrate as the terminal electron acceptor or as a nitrogen source. The mutants (Hno–) (i) formed neither soluble nor particulate hydrogenase antigens, (ii) expressed only about 50% the wild type level of ribulosebisphosphate carboxylase activity, and (iii) transported nickel, an essential constituent of active hydrogenase, at a significantly lower rate than wild type cells. Moreover, the mutants grew very slowly with urea as nitrogen source and did not express urease. Growth on formamide was also affected and formamidase activity was induced to only a very low level. Growth of the Hno– mutants on succinate, glutamate, fumarate, and malate was significantly slower than wild type, and a reduced rate of succinate incorporation into the mutant cells was demonstrated. The highly pleiotropic phenotype of Hno– mutants is indicative of a chromosomal gene with a considerable physiological importance. It affected the expression of both chromosomal and megaplasmid encoded systems of energy, carbon, and nitrogen metabolism. Thus, the hno mutation restricts the metabolic versatility but does not affect the basic metabolic functions of the organism. 相似文献
32.
Dr. Guy D. Fauque Yves M. Berlier Melvin H. Czechowski Bernard Dimon Paul A. Lespinat Jean LeGall 《Journal of industrial microbiology & biotechnology》1987,2(1):15-23
Summary Hydrogenases are among the main enzymes involved in bacterial anaerobic corrosion of metals. The study of their mode of action is important for a full comprehension of this phenomenon. The three types ofDesulfovibrio hydrogenases [(Fe), (NiFe), (NiFeSe)] present different patterns in the pH dependence of their activity. The periplasmic enzyme fromDesulfovibrio salexigens and the cytoplasmic enzyme fromDesulfovibrio baculatus both have pH optima at 7.5 for H2 uptake and 4.0 for H2 evolution and H+–D2 exchange reaction (measured by membrane-inlet mass-spectrometry). The H2 to HD ratio at pH above 5.0 is higher than 1.0. The periplasmic hydrogenase fromD. gigas presents the same pH optimum (8.0) for the H+–D2 exchange as for H2 consumption. In contrast, the enzyme fromD. vulgaris has the highest activity in H2 production and in the exchange at pH 5.0. Both hydrogenases have a H2-to-HD ratio below 1.0. 相似文献
33.
The respiratory system of chemolithoautotrophically-grown Alcaligenes latus contains a, b, and c type cytochromes. Two cytochrome oxidases were identified by their carbon monoxide difference spectra and their differing sensitivities to cyanide and carbon monoxide. The oxidases were cytochrome o and an a-type cytochrome. Ubiquinone was present in A. latus membranes and could be reduced by H2. The quinone analogue, 2-heptyl-4-hydroxy-quinoline-N-oxide (HQNO), was a strong inhibitor of the H2 oxidase reaction, but did not prevent the reduction of either ubiquinone or the cytochromes.Abbreviations HQNO
2-heptyl-4-hydroxy-quinoline-N-oxide
- TMPD
N,N,N,N-tetramethyl-p-phenylenediamine 相似文献
34.
35.
Thirty isolates of mungbean Rhizobium were tested for the presence of H2-recycling system. All the isolates were preliminary screened for detecting H2-recycling system in free culture using triphenyltetrazolium chloride reduction as screening procedure. The isolates which reduced the dye rapidly at early stages of growth were found to recycle hydrogen both in vivo as well as in vitro. Nitrogen fixing efficiency of hydrogenase positive, hydrogenase negative isolates and Hup– mutants was compared by green house experiments. There was 13–56% increase in dry matter and 21–46% increase in total nitrogen of the plants inoculated with H2-recycling isolates over the plants inoculated with non-recycling isolates. There was reduction in dry matter and total nitrogen content of the plants inoculated with Hup– mutants as compared to plants inoculated with wild type strain. The per cent decrease due to inoculation with Hup– mutants over wild type strain was 19–22 and 20–26 of dry weight and total nitrogen in plants, respectively.Abbreviations TTC
triphenyltetrazolium chloride 相似文献
36.
The ability of hydrogenases isolated from Thiocapsa roseopersicina and Lamprobacter modestohalophilus to reduce metal ions and oxidize metals has been studied. Hydrogenases from both phototrophic bacteria oxidized metallic Fe, Cd, Zn and Ni into their ionic forms with simultaneous evolution of molecular hydrogen. The metal oxidation rate decreased in the series Zn>Fe>Cd>Ni and depended on the pH. The presence of methyl viologen in the reaction system accelerated this process. T. roseopersicina and L. modestohalophilus cells and their hydrogenases reduced Ni(II), Pt(IV), Pd(II) or Ru(III) to their metallic forms under H2 atmosphere. These results suggest that metals or metal ions can serve as electron donors or acceptors for hydrogenases from phototrophic bacteria. 相似文献
37.
Several unicellular and filamentous, nitrogen-fixing and non-nitrogen-fixing cyanobacterial strains have been investigated on the molecular and the physiological level in order to find the most efficient organisms for photobiological hydrogen production. These strains were screened for the presence or absence of hup and hox genes, and it was shown that they have different sets of genes involved in H2 evolution. The uptake hydrogenase was identified in all N2-fixing cyanobacteria, and some of these strains also contained the bidirectional hydrogenase, whereas the non-nitrogen fixing strains only possessed the bidirectional enzyme. In N2-fixing strains, hydrogen was mainly produced by the nitrogenase as a by-product during the reduction of atmospheric nitrogen to ammonia. Therefore, hydrogen production was investigated both under non-nitrogen-fixing conditions and under nitrogen limitation. It was shown that the hydrogen uptake activity is linked to the nitrogenase activity, whereas the hydrogen evolution activity of the bidirectional hydrogenase is not dependent or even related to diazotrophic growth conditions. With regard to large-scale hydrogen evolution by N2-fixing cyanobacteria, hydrogen uptake-deficient mutants have to be used because of their inability to re-oxidize the hydrogen produced by the nitrogenase. On the other hand, fermentative H2 production by the bidirectional hydrogenase should also be taken into account in further investigations of biological hydrogen production.Abbreviations Chl
chlorophyll
- MV
methyl viologen 相似文献
38.
Ricardo O. Louro Teresa Catarino Carlos A. Salgueiro Jean LeGall António V. Xavier 《Journal of biological inorganic chemistry》1996,1(1):34-38
Using potentiometric titrations, two protons were found to participate in the redox-Bohr effect observed for cytochrome c
3 from Desulfovibrio vulgaris (Hildenborough). Within the framework of the thermodynamic model previously presented, this finding supports the occurrence
of a concerted proton-assisted 2e– step, ideally suited for the coupling role of cytochrome c
3 to hydrogenase. Furthermore, at physiological pH, it is shown that when sulfate-reducing bacteria use H2 as energy source, cytochrome c
3 can be used as a charge separation device, achieving energy transduction by energising protons which can be left in the acidic
periplasmic side and transferring deenergised electrons to sulfate respiration. This mechanism for energy transduction, using
a full thermodynamic data set, is compared to that put forward to explain the proton-pumping function of cytochrome c oxidase. 相似文献
39.
The localization of the dissimilatory sulfite reductase in Desulfovibrio desulfuricans strain Essex 6 was investigated. After treatment of the cells with lysozyme, 90% of the sulfite reductase activity was found in the membrane fraction, compared to 30% after cell rupture with the French press. Sulfite reductase was purified from the membrane (mSiR) and the soluble (sSiR) fractiion. On SDS-PAGE, both mSiR and sSiR exhibited three bands at 50, 45 and 11 kDa, respectively. From their UV/VIS properties (distinct absorption maxima at 391, 410, 583, 630 nm, enzymes as isolated) and the characteristic red fluorescence in alkaline solution, mSiR and sSiR were identified as desulfoviridin. Sulfite reductase (HSO3
-H2S) activity was reconstituted by coupling of mSiR to hydrogenase and cytochrome c
3 from D. desulfuricans. The specific activity of mSiR was 103 nmol H2 min-1 mg-1, and sulfide was the major product (72% of theoretical yield). No coupling was found with sSiR under these conditions. Furthermore, carbon monoxide was used to diferentiate between the membrane-bound and the soluble sulfite reductase. In a colorimetric assay, with photochemically reduced methyl viologen as redox mediator, CO stimulated the activity of sSiR significantly. CO had no effect in the case of mSiR. These studies documented that, as isolated, both forms of sulfite reductase behaved differently in vitro. Clearly, in D. desulfuricans, the six electron conversion HSO3
-H2S was achieved by a membranebound desulfoviridin without the assistance of artificial redox mediators, such as methyl viologen.Abbreviations
SiR
sulfite reductase
-
mSiR
sulfite reductase purified from membranes
-
sSiR
sulfite reductase purified from the soluble fraction
Enzymes Sulfite reductase, EC 1.8.99.1 Cytochrome c
3 hydrogenase, EC 1.12.2.1 相似文献
40.
The electron donor (component B) to the methyl coenzyme M methylreductase system from Methanosarcina thermophila was isolated as the 7-methyl derivative and characterized. Gas chromatography-mass spectrometry and 1H NMR analyses identified this derivative as 7-methylthioheptanoylthreonine phosphate (CH3-S-HTP), indicating that the original component B had the same structure (HS-HTP) as previously determined for component B from Methanobacterium thermoautotrophicum. The heterodisulfide of HS-HTP and coenzyme M (HS-CoM, 2-mercaptoethanesulfonate) was enzymatically reduced in cell extracts using electrons supplied by either H2 or CO, confirming that HS-HTP was a functional molecule in M. thermophila. 相似文献