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Showing 1 to 3 of 3 for “"flow-flash"”.
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Current understanding on cytochrome bd quinol oxidase of Escherichia coli a mutagenesis, kinetics and spectroscopic study
… 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 the enzyme from the rapid catalytic cycle of cytochrome bd …
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Biochemical characterization of C-family heme copper oxygen reductase
… during oxidation was further examined using the flow-flash technique. The results suggested that the proton transfer process involves two-steps: 1) proton transfer from an internal proton donor to the active site and 2) proton transfer from the bulk solution via the entrance (E49) of the …
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The interactions of cytochrome bo3 from Escherichia coli with its substrates - ubiquinone and oxygen
Heme-copper respiratory oxygen reductases reduce O2 to water and use the redox free energy to generate the proton motive force. 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 …