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Showing 1 to 11 of 11 for “"protoheme"”.

  1. Exploring Protoheme IX Farnesyltransferase as an Antimalarial Drug Target

    … characterized, including the gene encoding a protoheme IX farnesyltransferase (aka PfCOX10). This enzyme is a critical component of heme O synthesis. Since heme O is a necessary precursor to heme A, a critical cofactor of cytochromes within the mitochondrial electron transport chain (ETC), we …

    mit Repository record for Exploring Protoheme IX Farnesyltransferase as an Antimalarial Drug Target (opens in a new tab)

  2. Dynamics of Carbon-Monoxide Binding to Protoheme and Heme C Octapeptide

    Made available in DSpace on 2014-12-14T05:40:42Z (GMT). No. of bitstreams: 1 7714935.pdf: 2104594 bytes, checksum: ee7449340e5f60307a81e10719a0b16b (MD5) Previous issue date: 1977

    uiuc Repository record for Dynamics of Carbon-Monoxide Binding to Protoheme and Heme C Octapeptide (opens in a new tab)

  3. Dynamics of carbon monoxide binding to protoheme and heme c octapeptide

    Made available in DSpace on 2011-07-05T14:32:47Z (GMT). No. of bitstreams: 1 1977_chan.pdf: 2340958 bytes, checksum: d7a233669c5ad7b4e20e6fe3d2614510 (MD5) Previous issue date: 1977

    uiuc Repository record for Dynamics of carbon monoxide binding to protoheme and heme c octapeptide (opens in a new tab)

  4. The Purification and Characterization of The Cytochrome D Containing Terminal Oxidase of Escherichia Coli (Bioenergetics, Membranes, Ultracentrifugation)

    … cytochromes a(,1), b(,558) and d are present. Protoheme IX and heme d were the only prosthetic groups found in the complex, and iron was the only metal. This suggests that cythochrome a(,1) contains protoheme IX as a prosthetic group. Heme d is probably the site of oxygen binding, since both …

    uiuc Repository record for The Purification and Characterization of The Cytochrome D Containing Terminal Oxidase of Escherichia Coli (Bioenergetics, Membranes, Ultracentrifugation) (opens in a new tab)

  5. Pressure and temperature dependence of myoglobin kinetics

    … kinetics of carbon monoxide to myoglobin and protoheme are measured from 0.1 MPa to 190 MPa (1 bar to 1.9 kbar) at temperatures from 290K to 60K using flash photolysis. The role of the protein structure is elucidated by comparison of myoglobin kinetics with those of protoheme whose active …

    uiuc Repository record for Pressure and temperature dependence of myoglobin kinetics (opens in a new tab)

  6. Aspects of the hemes and modulation of hydrogen donors in catalases from bovine liver, yeast, and escherichia coli

    … Saccharomyces cerevisiae catalase enzymes are protoheme-containing, the HPII wild type protein contains heme d, and the mutant proteins contain either solely protoheme, or heme d-protoheme mixtures. Cyanide binding studies supported this, as ligand binding was monophasic for the bovine, …

    brock Repository record for Aspects of the hemes and modulation of hydrogen donors in catalases from bovine liver, yeast, and escherichia coli (opens in a new tab)

  7. Ultrafast studies of diffusion and electron transfer

    … to study the recombination of carbon monoxide to protoheme in glycerol:water over ten decades in time (1 ps to 10 ms). The rebinding consists of an initial nonexponential geminate phase followed by a slower exponential bimolecular phase. The entire time course of this reaction between 260 and 300 …

    uiuc Repository record for Ultrafast studies of diffusion and electron transfer (opens in a new tab)

  8. Localization of the prosthetic group ligands of cytochrome o terminal oxidase complex of Escherichia coli

    … has been purified and found to contain two protoheme IXs and one copper atom. Subsequently the gene encoding the cyo operon has been cloned. The research presented in this thesis focuses on the continued structural analysis of the cytochrome o oxidase complex including the following areas of …

    uiuc Repository record for Localization of the prosthetic group ligands of cytochrome o terminal oxidase complex of Escherichia coli (opens in a new tab)

  9. CHEMICAL AND PHYSICAL CHARACTERIZATION OF COMPLEX III; THE OXIDATIVE REACTION MECHANISM

    … can be represented by hindered bis-imidazole protoheme. The midpoint potentials for the b and c(,1) cytochrome were measured using MCD and EPR. A value of 270 mV was obtained for cytochrome c(,1) while the midpoint potentials found for the two species of cytochrome b varied with temperatures, …

    rice Repository record for CHEMICAL AND PHYSICAL CHARACTERIZATION OF COMPLEX III; THE OXIDATIVE REACTION MECHANISM (opens in a new tab)