Global ETD Search
Search theses and dissertations gathered from participating repositories worldwide. Every result links back to the library that holds it. No account is needed.
Results
Showing 1 to 20 of 56 for “"ubiquinone"”.
-
A double blind placebo controlled proving and comparative material medica of Ubiquinone
Submitted in partial compliance with the requirements for the Master’s Degree in Technology, Durban University of Technology, Durban, South Africa, 2015.
-
The interactions of cytochrome bo3 from Escherichia coli with its substrates - ubiquinone and oxygen
… enzyme contain between 0 to 2 equivalents of ubiquinone-8. Studies using ubiquinol-1, a soluble quinol substrate, indicate one high affinity quinone binding site, which acts as a non-exchanging co-factor, and a second, low-affinity site which is the substrate site. The residues interacting …
-
Inhibitor-Quinone Interactions in Reaction Centers From Rhodopseudomonas Sphaeroides (Herbicide, Triazine, Ubiquinone, Photosynthesis, Resistance)
The properties of ubiquinone and inhibitor binding to reaction centers (RCs) from the photosynthetic bacterium Rhodopseudomonas sphaeroides were studied. The charge recombination pathway between the primary electron donor, P, and the primary ubiquinone electron acceptor, Q(,A), or the secondary …
-
Studies of Lipid Metabolism: I. The Effect of Vitamin E Deficiency, Fattyacid Deficiency and Dietary Cholesterol on The Ubiquinone Concentration in The Liver. Ii. The Metabolism of 1-Carbon-14-Methyl Linoleate Hydroperoxide in The Rabbit
Made available in DSpace on 2014-12-09T14:28:49Z (GMT). No. of bitstreams: 1 6507123.pdf: 2658708 bytes, checksum: 0d61ccd7f5e079735d5532a43d016db3 (MD5) Previous issue date: 1965
-
EPR and solid-state NMR studies on the mechanism of cytochrome bo3 ubiquinol oxidase from escherichia coli
… the ubiquinol pool are first transferred to a ubiquinone cofactor bound at the high affinity binding site known as the QH-site, from which electrons are moved one at a time sequentially to the low-spin heme b and the CuB-heme o3 catalytic site. In this study, E. coli C43(DE3) auxotroph strains …
-
Moessbauer Studies of Photosynthetic Reaction Centers From Rhodopseudomonas Sphaeroides R-26
… reaction centers (RCs) differing in ubiquinone content, detergent, oxidation state, or the presence of o-phenanthroline all show a single quadrupole doublet of similar splitting (DELTA)E(,Q), center shift (delta), and temperature dependence. The results are indicative of high-spin …
-
Molecular genetic studies of the cytochrome o terminal oxidase complex in Escherichia coli
… enzyme catalyzes the oxidation of ubiquinol-8 to ubiquinone-8 within the cytoplasmic membrane and the concomitant reduction of O$\sb2$ to H$\sb2$O. Cytochrome $o$ oxidase has been purified and shown to contain four subunits on SDS-PAGE gels. The cloning of the $cyo$ operon makes it possible to …
-
Biochemical characterization of a-type heme-copper oxidases in escherichia coli, bacillus subtilis and thermus thermophilus
… (Arg71, Asp75, His98, and Gln101) involved in ubiquinone semiquinone radical stabilization at quinone binding site in E. coli cytochrome bo3 oxidase. Similar result was reported on cytochrome aa3-600 oxidase in B. subtilis, a close homolog to cytochrome bo3 that uses menaquinone instead of …
-
Deconvoluting the Engineering and Assembly Instructions for Complex Iii Activity
… Complex III catalyzes the oxidation of ubiquinone and the reduction of a soluble cytochrome with the bioenergetic formation of a transmembrane proton gradient (∆μH+). Complex III turnover is initiated by a unique two electron oxidation of ubiquinone at the Qo site; one electron is …
-
Molecular Studies of the Succinate:ubiquinone Oxidoreductase of Escherichia Coli
Succinate:ubiquinone oxidoreductase (Complex II) is a membrane-bound enzyme present in aerobically grown bacteria and in the mitochondria of eukaryotes. It functions as succinate dehydrogenase in the citric acid cycle and transfers reducing equivalents to ubiquinone in the aerobic electron …
-
Electron Transfer in the Reaction Center From Rhodopseudomonas Viridis (Photosynthesis, Bioenergetics, Bacteria)
… and the secondary quinone, Q(,B), as a ubiquinone. The forward electron transfer equilibrium, from Q(,A) to Q(,B), was found to be driven by a large enthalpy decrease which compensated a decrease in entropy. This electron transfer was inhibited by some herbicides which act at Photosystem …
-
Heterogeneity of the Bc1 Complex Subunits and Qo Site Occupants From Rhodobacter Sphaeroides
… complex in the presence of bacterial succinate-ubiquinone reductase and appropriate quinones was developed to characterize the best samples for crystallization based on enzymatic activity. The presence of all cofactors in bc1 complex is required for proper function and is required to be of …
-
Using molecular approaches to understand Complex I deficiency in mouse models
Complex I (NADH:ubiquinone oxidoreductase), a major electron entry point to the mitochondrial respiratory chain, couples electron transfer from NADH to ubiquinone to proton pumping across the mitochondrial inner membrane, and generates the proton motive force that drives ATP synthesis and transport …
-
Structural Studies into the Mechanism and Organisation of Mammalian Respiratory Complex I
Respiratory complex I (NADH:ubiquinone oxidoreductase) is the major entry point of electrons into the electron transport chain and couples its redox activity with proton pumping across the inner mitochondrial membrane, thus contributing to the proton motive force which drives ATP synthesis. With …
-
Investigations of the mechanism of mitochondrial complex I by electron cryomicroscopy
… The first enzyme in the ETC is complex I (NADH:ubiquinone oxidoreductase). Complex I oxidises NADH in the matrix, reduces ubiquinone in the inner membrane, and couples the energy released to the translocation of four protons across the inner membrane, generating the proton motive force that …
-
Paracoccus denitrificans as a model system for studying the mechanism of respiratory complex I
Respiratory complex I (NADH:ubiquinone oxidoreductase) is a crucial metabolic enzyme that couples the free energy released from NADH oxidation and ubiquinone reduction to the translocation of four protons across an energy-transducing membrane, contributing to the proton motive force used to …
-
Structure-function studies of respiratory complex I from Paracoccus denitrificans using membrane mimetics
Respiratory complex I (NADH:ubiquinone oxidoreductase) is a crucial metabolic enzyme that couples the free energy released from NADH oxidation and ubiquinone reduction to translocate four protons across energy-transducing membranes, contributing to the proton motive force that powers oxidative …
-
Characterizations on bacterial photosynthesis and respiration with optical spectroscopy and magnetic resonance
… HA- (bacteriopheophytin in the A branch) to QA (ubiquinone in the A branch) and back electron transfer from QA- to P+ (special pair of bacteriochlorophyll). Both electron transfers slows down by about 4 fold at room temperature. I have also examined the reactivity of the semiquinones in the LM …
-
Cryo-EM studies of substrate and inhibitor binding to mammalian respiratory complex I
Mammalian respiratory complex I (NADH:ubiquinone oxidoreductase) is an intricate multi-subunit, energy-transducing membrane protein that is essential for aerobic energy metabolism and NADH/NAD⁺ homeostasis. It couples the energy released from NADH oxidation and ubiquinone (Q) reduction to pump four …
-
Increasing Heterologous Protein Secretion From the Yeast S. Cerevisiae Through Manipulation of Cellular Redox Factors
… did not increase BPTI secretion. The addition of ubiquinone, which has been shown to be an electron acceptor from the E. coli disulfide bond formation chain, increased BPTI secretion from cultures overexpressing FMO, but under no other scenarios. A system has been set up to utilize the yeast …
Page 1 of 3