Sulfide oxidation by gene expressions of sulfide-quinone oxidoreductase and ubiquinone-8 biosynthase in Escherichia coli.

  title={Sulfide oxidation by gene expressions of sulfide-quinone oxidoreductase and ubiquinone-8 biosynthase in Escherichia coli.},
  author={Hiroomi Shibata and M. Takahashi and I Yamaguchi and S. Kobayashi},
  journal={Journal of bioscience and bioengineering},
  volume={88 3},
Menaquinone reduction by an HMT2-like sulfide dehydrogenase from Bacillus stearothermophilus.
The gene-encoding HMT2-like sulfide dehydrogenase from Bacillus stearothermophilus JCM2501 was amplified and expressed in Escherichia coli and the enzymatic features were examined and sulfide oxidation via MK in the cellular membrane of Gram-positive bacteria was certified.
Occurrence, biosynthesis and function of isoprenoid quinones.
Biosynthesis, bioproduction and novel roles of ubiquinone.
  • M. Kawamukai
  • Biology, Chemistry
    Journal of bioscience and bioengineering
  • 2002
Sulfide Oxidation Evidences the Immediate Cellular Response to a Decrease in the Mitochondrial ATP/O2 Ratio
The consequences of sulfide oxidation by mitochondrial sulfide quinone reductase in mammalian cells are examined, finding that if oxygen supply or respiratory chain activity becomes a limiting factor, small variations in sulfide release impact the cellular ATP/ADP ratio, a major metabolic sensor.
C. elegans RHY-1 and CYSL-1 act independently of HIF-1 to promote survival in hydrogen sulfide
A novel function of RHY-1 is revealed, which is independent of hif-1, that protects against toxic effects of H2S, and is shown to act in concert with CYSL- 1, an orthologue of human cystathionine β-synthase, to promote survival in H1S.
Metabolism of Natural Polymeric Sulfur Compounds
Introduction Historical Outline Chemical Structures Hydrogen Sulfide and Inorganic Polysulfides Chemistry, Structures and Characterization Occurrence Metabolism under Oxidative Conditions


Sulfide oxidation in the phototrophic sulfur bacterium Chromatium vinosum
Investigation of sulfide oxidation in the phototrophic purple sulfur bacterium Chromatium vinosum D showed that the sulfide:quinone oxidoreductase activity was sensitive to heat and to quinone analogue inhibitors, and the enzyme is strictly membrane-bound and is constitutively expressed.
Sulfide-Quinone Reductase from Rhodobacter capsulatus
The complete sequence of the SQR from R. capsulatus shows further similarity to flavoproteins, in particular glutathione reductase and lipoamide dehydrogenase.
A C-methyltransferase involved in both ubiquinone and menaquinone biosynthesis: isolation and identification of the Escherichia coli ubiE gene
The transformation of a strain harboring the ubiE401 mutation with o251 on an expression plasmid restored both the growth of this strain on succinate and its ability to synthesize both ubiquinone and menaquinone.
A novel membrane-bound flavocytochrome c sulfide dehydrogenase from the colourless sulfur bacterium Thiobacillus sp. W5
Abstract A novel membrane-bound sulfide-oxidizing enzyme was purified 102-fold from the neutrophilic, obligately chemolithoautotrophic Thiobacillus sp. W5 by means of a six-step procedure. Spectral
Physiology and genetics of sulfur-oxidizing bacteria.
Existence of a Hydrogen Sulfide:Ferric Ion Oxidoreductase in Iron-Oxidizing Bacteria
It was found that hydrogen sulfide:ferric ion oxidoreductase activity comparable to that of T. ferrooxidans AP19-3 was present in all iron-oxidizing bacteria tested, suggesting a wide distribution of this enzyme in iron- oxidizingacteria.
Biochemical and Genetic Studies on Ubiquinone Biosynthesis in Escherichia coli K-12: 4-Hydroxybenzoate Octaprenyltransferase
The results of genetic analysis suggest that each of the ubiquinone-deficient mutants of Escherichia coli carries a mutation in a gene designated ubiA which can be represented at minute 79 on the E. coli chromosome map, which suggested that the ubiB gene is the structural gene coding for this enzyme.