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Showing 1 to 12 of 12 for “"Terminal oxidases"”.
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Spectroscopic analysis and dynamics of ligand binding to bacterial oxidases
… chain of Escherichia 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 …
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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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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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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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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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Microscopic description of gas permeation and delivery pathways in biological macromolecules
… of O2, NO and CO2 in aerobic respiratory terminal oxidases (cytochrome ba3 and cytochrome aa3), nitric oxide reductase (cNOR) and bacterial carboxysome, and to describe the movement of O2, CO2 and NH3 through lipid membranes and membrane channels. In the first part of this dissertation, I …
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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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Localization of a quinol oxidase domain of the cytochrome d complex of Escherichia coli
… chain of Escherichia coli contains two terminal oxidases, the cytochrome d complex and the cytochrome o complex. 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 …
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Simulation studies of the structure-function relationship of two biological processes: proton pumping in cbb3 oxidase and activation of Parkin
… 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 translocation of protons across the membrane, a process that is essential for …
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Studies of proton pumping mechanism in BA3 type cytochrome oxidase of thermus thermophilus and CBB3 type cytochrome oxidase of vibrio cholerae
… in which the cbb3 oxygen reductases are the only terminal oxidases in their respiratory chains, and the γ- proteobacterium Pseudomonas stutzeri.
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Engineering heme-copper and multi-copper oxidases for efficient oxygen reduction catalysis
… frequency and low overpotential Heme-copper oxidases catalyze four-electron reduction of oxygen to water, and the energy harvested is utilized to drive the synthesis of adenosine triphosphate. While much effort has been made to design a catalyst mimicking the function of terminal oxidases, …
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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
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, …