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 9 of 9 for “"cytochrome bo3"”.
-
The interactions of cytochrome bo3 from Escherichia coli with its substrates - ubiquinone and oxygen
… 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 2 equivalents of ubiquinone-8. …
-
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 …
-
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 …
-
Biochemical characterization of a-type heme-copper oxidases in escherichia coli, bacillus subtilis and thermus thermophilus
… by far the most abundant including mitochondrial cytochrome c oxidase and its close homologs. Over the years, great efforts have been invested to study the function of A-type oxidases. A highly conserved glutamic acid residue has been proved to be the branch point for proton translocation, …
-
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
Cytochrome c oxidases (CcO) are terminal oxidases in the respiratory chain and contribute to a large fraction in the heme-copper oxidase superfamily. They are transmembrane protein complexes catalyzing the reduction of dioxygen to water with a variety range of electron donors. During the process, …
-
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 …
-
Exploring the Structure-Function Relationships and Dynamics of the Heme/copper Oxidase Superfamily Using Cytochrome Bo(3) From Escherichia Coli as a Model System
… results are shown, which demonstrate that cytochrome bo3 can be constituted into stable thin films, suitable for ATR-FTIR work.
-
Examining Molecular Interactions of Proteins by Isotopic Labeling, Sample Formulation and Solid-State NMR Spectroscopy
… methods of two large membrane proteins, E. coli cytochrome bo3 oxidase and A. thaliana cytochrome P450 monooxygenase 98A3. To obtain site-specific resolution in uniformly- 13C, 15N labeled samples of these proteins, hardware advances, new experimental techniques and increased dimensionality were …
-
Solid-state NMR studies of membrane proteins and membrane protein complexes
… SSNMR techniques 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.