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Showing 1 to 11 of 11 for “"ubiquinol oxidase"”.
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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
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, …
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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
… 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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Identification and Characterization of the Cyd Gene Locus of Escherichia Coli (Respiration, Membranes, Cloning, Energetics, Cytochromes)
… 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 developed …
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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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Interfacial modulation of protein function explored through atomistic molecular dynamics simulation
… sphaeroides and the quinone-binding site of ubiquinol oxidase. Recent structural work on the polyaromatic cation transporter EmrE, and its electrostatic locking mechanism governing conformational change, are also discussed. Interactions at the interface of cellulose have also been simulated. …
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Biochemical characterization of a-type heme-copper oxidases in escherichia coli, bacillus subtilis and thermus thermophilus
Heme-copper oxidases (HCOs) couple the free energy of oxygen reduction and translocate protons across membrane to generate a proton electrochemical gradient, which was used to produce ATP by ATP synthase. Based on the sequences and structures of core subunits, they are classified into 3 types. …