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Showing 1 to 3 of 3 for “"Iron-sulfur flavoprotein"”.

  1. Biochemical characterization of a novel iron-sulfur flavoprotein from Methanosarcina thermophila strain TM-1

    The iron-sulfur flavoprotein (Isf) from the acetate utilizing methanoarchaeon Methanosarcina thermophila was heterologously produced in Escherichia coli, purified to homogeneity, and characterized to determine the properties of the iron-sulfur cluster and FMN. Chemical and spectroscopic analyses …

    vt Repository record for Biochemical characterization of a novel iron-sulfur flavoprotein from Methanosarcina thermophila strain TM-1 (opens in a new tab)

  2. Characterization of the genes and gene products of the acetate-activating enzymes and a novel iron-sulfur flavoprotein from Methanosarcina thermophila strain TM-1

    The genes encoding the acetate kinase and phosphotransacetylase enzymes from <i>Methanosarcina thermophila</i> were isolated from a genomic library on a fifteen kilobase fragment The genes are located adjacent to one another, with the phosphotransacetylase gene (<i>pta</i>) directly upstream of the …

    vt Repository record for Characterization of the genes and gene products of the acetate-activating enzymes and a novel iron-sulfur flavoprotein from Methanosarcina thermophila strain TM-1 (opens in a new tab)

  3. Genetic and Biochemical Characterization of the Heteromeric Dihydroorotate Dehydrogenase From Bacillus Subtilis

    … formed a heteromeric DHOD holoenzyme, an iron-sulfur flavoprotein which was determined by gel filtration to be a tetramer containing 2 mol PyrDI and 2 mol PyrDII. The two subunits were also overexpressed individually and purified. Overexpressed PyrDII formed inclusion bodies and could be …

    uiuc Repository record for Genetic and Biochemical Characterization of the Heteromeric Dihydroorotate Dehydrogenase From Bacillus Subtilis (opens in a new tab)