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Showing 1 to 11 of 11 for “"cytochrome bd"”.
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Mutagenesis and Spectroscopic Studies on Cytochrome Bd Quinol Oxidase of Escherichia Coli
… studies on the highly conserved residues of cytochrome bd quinol oxidase from Escherichia coli were carried out to investigate their roles in maintaining structure and function of this enzyme. Mutations on two highly conserved residues in subunit I---Glu445 and Arg391 were characterized in …
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Structure-function relationship studies of the cytochrome bd oxidase of Escherichia coli
The cytochrome bd oxidase complex is one of two terminal oxidases which are components of the aerobic respiratory chain of Escherichia coli. This membrane-bound oxidase catalyzes the two-electron oxidation of ubiquinol and the four-electron reduction of oxygen to water. Enzyme turnover generates …
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An Investigation of Cytochrome Bd Quinol Oxidases of Vibrio Cholerae, Rhodobacter Sphaeroides, and Salmonella Typhimurium
… harbor an oxidase that is distinct from the bd-I oxidase of E. coli . Chapter five lays out the development of a flow cytometry assay that can be used to study bacterial membrane polarization. This assay is a specific, rapid, and efficient method to screening potential ionophores and …
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Current understanding on cytochrome bd quinol oxidase of Escherichia coli a mutagenesis, kinetics and spectroscopic study
Time-resolved kinetics study on the cytochrome bd quinol oxidase from Escherichia coli was carried out by stopped-flow techniques. The natural substrate, ubiquinol, was used to turnover the enzyme in the fast catalysis successfully for the first time. The results excluded the fully oxidized form of …
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Structure and Function Relationships in Cytochrome Bo(3) Oxidase and Cytochrome Bd-I Oxidase From Escherichia Coli
… 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 turnover stops, the enzyme is found in a mixture of oxidation …
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Studies on the cytochrome bd-type oxygen reductase superfamily and the discovery of a novel nitric oxide reductase
… all aerobic respiration on the planet– the bd-type oxygen reductase superfamily and the heme-copper oxidoreductase superfamily. The bd-type oxygen reductases are present in bacteria and archaea and catalyze the 4-electron reduction of oxygen to water. Electrons from membrane bound quinols …
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Using myoglobin models of oxidases for mechanistic understanding of the oxygen reduction reaction
… the role of heteronuclear metal active sites. Cytochrome bd oxidase models have been used to make sense of many interesting – but isolated – observations of these peculiar enzymes. These studies come at a serendipitous time for cytochrome bd oxidases, as a recent discovery has made experts in …
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Spectroscopic analysis and dynamics of ligand binding to bacterial oxidases
… coli contains two terminal oxidases, the cytochrome bd complex and the cytochrome 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 …
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Characterizing the Role of the E. Coli Cytochrome Oxidase AppBCX During Intestinal Inflammation
… have studied the physiological function of the cytochrome bd oxidase, AppBCX. Using both chemical and genetic models of non-infectious colitis we have shown that it allows E. coli to utilize low levels of oxygen early in inflammation. Additionally, we have characterized the regulation of this …
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Repurposing chlorpromazine and its metabolites for antituberculosis drug discovery
… the use of RIF with M3 and M5, bedaquiline (BDQ) with M2, and SPEC with M3 were bactericidal. At 140μM, CPZ and M1, M2, M3 treated samples exhibited a 2-fold up-regulation of the cydA (Rv1623c) gene which encodes an essential subunit of the cytochrome bd-type menaquinol oxidase in Mtb. The …