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.
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Showing 1 to 20 of 20 for “"terminal oxidase"”.
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Pyruvate Oxidase and the Cytochrome D Terminal Oxidase of Escherichia Coli
… electron transport system were studied, pyruvate oxidase and the cytochrome d terminal oxidase. Three general subjects were treated: (i) the active site structure and catalytic mechanism of pyruvate oxidase, (ii) the role of pyruvate oxidase in the E. coli aerobic electron transport system, and …
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Purification and Characterization of the Cytochrome-O Containing Terminal Oxidase of Escherichia Coli
The function of the aerobic respiratory chain of E. coli is to convert the energy released by the transfer of electrons from substrate molecules to oxygen into a proton gradient that can be used by the cell for ATP synthesis, locomotion and active transport of ions and molecules into and out of the …
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Molecular genetic studies of the cytochrome o terminal oxidase complex in Escherichia coli
The cytochrome $o$ terminal oxidase complex is a component of aerobic respiratory chain of Escherichia 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 …
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Molecular Biology of the Cytochrome O Terminal Oxidase of Escherichia Coli (Cloning, Sequencing, Dna)
… a genetic approach to studying the cytochrome o terminal oxidase complex of Escherichia coli. Respiratory-deficient mutants of E. coli have been isolated which are unable to grow aerobically on non-fermentable substrates such as succinate and lactate. Spectroscopic and immunological studies …
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Isolation and characterization of new mutants of the cytochrome d terminal oxidase of Escherichia coli
The cytochrome d terminal oxidase from Escherichia coli is a two-subunit, three-heme integral membrane cytochrome. Subunit I contains the heme center $b\sb{558}$ and Subunit II, is necessary for the binding of the $b\sb{595}$ and d heme prosthetic groups. Earlier work suggests that the N-terminus …
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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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The Purification and Characterization of The Cytochrome D Containing Terminal Oxidase of Escherichia Coli (Bioenergetics, Membranes, Ultracentrifugation)
The cytochrome d-containing terminal oxidase of Escherichia coli has been purified to at least 90% of homogeneity, judging from the Coomassie blue staining of SDS-polyacrylamide gels. These gels showed that the cytochrome contained two types of subunits with molecular weights of 57,000 Daltons and …
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Analysis of the topology of the cytochrome d terminal oxidase complex of Escherichia coli by genetic methods
The cytochrome d terminal oxidase is one of two terminal oxidases in the aerobic respiratory chain of E. coli. The topology of the two subunits of the complex were examined by the use of alkaline phosphatase gene fusions, and models proposed. The expression and assembly of the subunits was also …
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Molecular Studies of the NADH:ubiquinone Oxidoreductases and Thebo-Type Terminal Oxidase of the Aerobic Respiratory Chain of Escherichia Coli
… two 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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The Mechanism of Aerotaxis in SALMONELLA TYPHIMURIUM
… <p>The receptor for aerotaxis was the major terminal oxidase of the electron transport system. The evidence supporting this conclusion was 1) the K<sub>0.5</sub> of the aerotaxis receptor (K<sub>0.5</sub> = 0.7 μM) and the K<sub>m</sub> of the terminal oxidase (K<sub>m</sub> = 0.7 μM) were …
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Structure and Function Relationships in Cytochrome Bo(3) Oxidase and Cytochrome Bd-I Oxidase From Escherichia Coli
Structure and function relationships in the two terminal oxidases in Escherichia coli have been investigated. Cytochrome bo3 oxidase, a member of the heme/copper superfamily, is found to have a semiquinone intermediate during turnover of quinol. Additionally, after the quinol is consumed and …
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Simulation studies of the structure-function relationship of two biological processes: proton pumping in cbb3 oxidase and activation of Parkin
… of two important enzymes: a C-type cytochrome c oxidase (cbb3) and an E3 ubiquitin ligase (Parkin).<br/><br/>Cbb3 is a C-type terminal oxidase responsible for catalyzing the final step of aerobic respiration (namely the reduction of oxygen to water) and coupling this redox reaction to the active …
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Identification and Characterization of the Cyd Gene Locus of Escherichia Coli (Respiration, Membranes, Cloning, Energetics, Cytochromes)
… transport chain of Escherichia coli contains a terminal oxidase, cytochrome d, which is part of a two subunit protein complex that is composed of two additional cytochromes, b(,595) and b(,558). The first mutants affecting the cytochrome d complex (Cyd) have been isolated using two newly …
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Molecular biology studies on thecyd operon of Escherichia coli
The Cytochrome d terminal oxidase complex is one of two terminal oxidases in the aerobic respiratory chain of Escherichia coli. The enzyme is located in the cytoplasmic membrane where it oxidizes ubiquinol-8 and reduce oxygen to water. The enzyme is an $\alpha\beta$ hetero-dimer containing hemes …
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Studies of Three Human Intestinal Opportunistic Pathogens
… both virulence factors CNF1 and HlyA, the terminal oxidase cytochrome o, or a double cyo/cyd mutant were, deficient in survival in the spleen, but not the liver of BALB/c mice.
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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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Lipopolysaccharide, K antigen, and other components of the bacterial cell surface important for S. meliloti-alfalfa symbiosis
… vitamin B12 , or cobalamin; QxtA, a predicted terminal oxidase of respiration; a predicted magnesium and cobalt transporter; and the process of carbon fixation. Undoubtedly the genes, factors, and metabolic processes identified in these studies will lead to a greater understanding of the …
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CHARACTERIZATION OF LOW MOLECULAR WEIGHT C-TYPE CYTOCHROMES IN CYANOBACTERIA AND PLANTS
… Cyt b6f complex to Photosystem I (PSI) or the terminal oxidase, and in plants Pc transfers electrons from the Cyt b6f complex to PSI. Along with Pc or Cyt c6, additional, poorly uncharacterized, low molecular weight electron carriers have recently been reported in cyanobacteria, algae and …
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Optimizing electrogenic activity from photosynthetic bacteria in bioelectrochemical systems
… nitric oxide reductase – NorB, cytochrome-c oxidase – COX, bd-quinol oxidase – cyd, and the respiratory terminal oxidase – ARTO, roughly doubled light driven electron flux to EET. Deletion of nitrate reductase – NarB, and nitrite reductase – NirA, increased EET to a similar degree, but …
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The interactions of cytochrome bo3 from Escherichia coli with its substrates - ubiquinone and oxygen
… the heme-copper oxygen reductases are the quinol oxidases, 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 …