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Showing 1 to 20 of 32 for “"ubiquinol"”.
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Effects of Ubiquinol with Fluid Resuscitation following Hemorrhagic Shock
… apoptosis and contribute to organ dysfunction.1 Ubiquinol is a potent free radical scavenger which is produced endogenously and functions as part of the mitochondrial respiratory chain.2 No study has been conducted to investigate the effects of ubiquinol related to HS. The overall aim of this …
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Electron Transfer Reactions of the Ubiquinol: Cytochrome C-2 Oxidoreductase of Rhodopseudomonas Sphaeroides
The electron transfer reactions of the ubiquinol:cytochrome c(,2) oxidoreductase (b-c(,1) complex) of the photosynthetic bacteria Rps. sphaeroides have been investigated through the use of optical spectroscopy and chemical inhibitors of the protein complex.
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Exploration of the molecular structure of Escherichia coli cytochrome bo ubiquinol oxidase by genetic approach
Cytochrome bo ubiquinol oxidase is one of the two terminal ubiquinol oxidases in the aerobic respiratory chain of Escherichia coli. By deleting the intergenic region between the cyoA and cyoB and one base in the overlapping sequence between cyoB and cyoC, in-frame fusions are made between all three …
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EPR and solid-state NMR studies on the mechanism of cytochrome bo3 ubiquinol oxidase from escherichia coli
Cytochrome bo3 ubiquinol oxidase from E. coli is a member of heme-copper oxidase superfamily. This trans-membrane enzyme complex catalyzes two-electron oxidation of ubiquinol and reduction of molecular oxygen to water. During the process, the protons from ubiquinol are released to the periplasmic …
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Structural and Functional Studies on Cytochrome BO3 Ubiquinol Oxidase From Escherichia Coli and the Characterization of Its Quinone Binding Sites
Cytochrome bo3 ubiquinol oxidase is the terminal oxidase in the aerobic respiratory chain of Escherichia coli. The enzyme catalyzes the oxidation of ubiquinol-8 and the reduction of oxygen to water, which are coupled to the translocation of protons across the cytoplasmic membrane via protolytic …
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Studies on the structure, function and mechanisms of the cbb3 type cytochrome c oxidase from Vibrio cholerae and the cytochrome bo3 ubiquinol oxidase from Escherichia coli
… c oxidase from V. cholerae and bo3 type ubiquinol oxidase from E. coli were investigated separately. Site directed mutagenesis were carried out in the case of cbb3 protein based on crystal structure and sequence alignment. Activity data suggested that the D pathway analogue is blocked …
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Structure-function relationship studies of the cytochrome bd oxidase of Escherichia coli
… oxidase catalyzes the two-electron oxidation of ubiquinol and the four-electron reduction of oxygen to water. Enzyme turnover generates proton and voltage gradients across the bilayer. The oxidase is a heterodimer containing three heme prosthetic groups, $b\sb{558},$ $b\sb{595},$ and d. To …
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Localization of a quinol oxidase domain of the cytochrome d complex of Escherichia coli
… Each of these enzymes catalyzes the oxidation of ubiquinol-8 within the cytoplasmic membrane and the reduction of molecular oxygen to water. Both oxidases are coupling sites in the respiratory chain. The cytochrome d complex is a heterodimer (subunits I, II) which has three heme prosthetic groups. …
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Molecular Studies of the NADH:ubiquinone Oxidoreductases and Thebo-Type Terminal Oxidase of the Aerobic Respiratory Chain of Escherichia Coli
… NADH:ubiquinone oxidoreductases and a terminal ubiquinol oxidase, from the respiratory chain of the bacterium Escherichia coli are addressed in this thesis. These three enzymes were examined by a variety of genetic and spectroscopic techniques.
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Spectroscopic analysis and dynamics of ligand binding to bacterial oxidases
… bo complex. Each of these enzymes functions as a ubiquinol oxidase and reduces molecular oxygen to water. Although the two enzymes perform the same function they do not show any obvious similarity between their gene sequences and therefore, their structure. This thesis addresses the differences …
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Molecular genetic studies of the cytochrome o terminal oxidase complex in Escherichia coli
… coli. This 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 …
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Localization of the prosthetic group ligands of cytochrome o terminal oxidase complex of Escherichia coli
The cytochrome o ubiquinol oxidase is one of two terminal oxidases present in the aerobic respiratory chain of E. coli. The cytochrome o complex 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 …
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Analysis of heme-copper ligation, quinol activity, and ligand binding kinetics of cytochrome BO(3) quinol oxidase from E. coli
… were interpreted with respect to heme content, ubiquinol content, absolute absorption spectra, ligand bound absorption spectra, and ligand binding kinetics. Structural and functional perterbations by the mutation of conserved residues were determined with ligand binding kinetics. Finally, …
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Characterization of alternative NADH dehydrogenases in the respiratory chain of Toxoplasma gondii as a novel drug targets
… wobei der Inhibitor wahrscheinlich mit der Ubiquinol Bindungsstelle des Enzyms interferiert. In dieser Studie konnte in Zellkulturversuchen die Inhibition der Replikation von T. gondii dargestellt werden. Die IC50 wurde mit zwei unabhängigen Wachstumsassays bestimmt und lag zwischen ~2-8 nM. …
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Identification and Characterization of the Cyd Gene Locus of Escherichia Coli (Respiration, Membranes, Cloning, Energetics, Cytochromes)
… native state. Purified cytochrome b(,558) is a ubiquinol oxidase, but it does not reduce molecular oxygen. The measured extinction coefficient of 21,000 M('-1) cm('-1) indicates a 1:1 stoichiometry of cytochrome b(,558) per Cyd.
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Estudio sobre la expresión de oxidasa alternativa en yemas de vid cv. Thompson seedles durante el período de eco y endodomancia
… en Elqui. La Oxidasa Alternativa (AOX) es una ubiquinol oxidasa, ubicada en la membrana interna de la m¡tocondria de plantas, que entrega los electrones cedidos por el ubiquinol directamente al oxÍgeno para formar agua sin aumentar el gradiente transmembrana de protones, produciendo de este …
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The interactions of cytochrome bo3 from Escherichia coli with its substrates - ubiquinone and oxygen
… which catalyze the 2-electron oxidation of ubiquinol or menaquinol instead of cytochrome c. Escherichia coli (E. coli) cytochrome bo3 is the best characterized quinol oxidase. Depending on the detergent used to solubilize the enzyme, cyt bo3, preparations of this enzyme contain between 0 to …
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Purification and Characterization of the Cytochrome BC(1) Complex From Rhodobacter Sphaeroides
A highly active, large-scale preparation of ubiquinol:cytochrome $c\sb2$ oxidoreductase (cytochrome $bc\sb1$ complex) has been obtained from Rhodobacter sphaeroides. The enzyme was extracted from chromatophores using dodecyl maltoside in the presence of glycerol, and was purified by anion exchange …
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Molecular biology studies on thecyd operon of Escherichia coli
… in the cytoplasmic membrane where it oxidizes ubiquinol-8 and reduce oxygen to water. The enzyme is an $\alpha\beta$ hetero-dimer containing hemes $b\sb{558}$, $b\sb{595}$ and d. The cyd locus, which encodes both subunits, has been cloned and mapped genetically. The thesis research described …
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Solid-state NMR studies of membrane proteins and membrane protein complexes
… are used to study a 144 kDa cytochrome bo3 ubiquinol oxidase demonstrating the power of this technique to investigate large membrane complexes in native environments.
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