Global ETD Search
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Showing 1 to 9 of 9 for “"Quinol oxidase"”.
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Mutagenesis and Spectroscopic Studies on Cytochrome Bd Quinol Oxidase of Escherichia Coli
… 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 detail. Mutant …
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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 in the …
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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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Analysis of heme-copper ligation, quinol activity, and ligand binding kinetics of cytochrome BO(3) quinol oxidase from E. coli
… type and mutant forms of cytochrome $bo\sb3$ quinol oxidase from E.coli were examined. Structural properties of subunit II were addressed with the restoration of the putative Cu$\sb{\rm A}$ ligands and construction of a chimeric E.coli/R.sphaeroides subunit II. Functional properties of subunit …
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Structural and Functional Studies of the Cytochrome D Oxidase Complex of Escherichia Coli
The cytochrome d oxidase complex is one of two terminal quinol oxidase complexes of Escherichia coli. The heterodimeric complex contains three heme prosthetic groups, $b\sb{558}, b\sb{595},$ and d. Two histidines, His19 and His186, in subunit I are essential for retaining the heme groups. His19 was …
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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
… Among 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 …
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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. …