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- W2032907492 abstract "The C-terminal periplasmic domain of subunit II of the Escherichia coli bo-type ubiquinol oxidase was replaced with the counterpart of the thermophilic Bacillus caa3-type cytochrome c oxidase containing the CuA-cytochrome c domain by means of gene engineering techniques. The chimeric terminal oxidase was expressed by a pBR322 derivative in a terminal oxidase deficient mutant of E. coli, although the amount of the chimeric enzyme was smaller than that of the Escherichia coli bo-type ubiquinol oxidase expressed by the original cytochrome bo-expressing plasmid. The chimeric enzyme showed much higher TMPD (N,N,N',N'-tetramethyl-p-phenylenediamine) oxidase activity than the wild-type cytochrome bo, but lower activity than the thermophilic Bacillus caa3-type cytochrome c oxidase. The chimeric subunit II was confirmed to bind to heme C. These results suggest that the CuA-cytochrome c domain grafted to this membrane anchor can facilitate electron transfer from reduced TMPD to low-spin protoheme b in subunit I." @default.
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- W2032907492 date "1997-11-01" @default.
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- W2032907492 title "Expression of the Escherichia coli bo-Type Ubiquinol Oxidase with a Chimeric Subunit II Having the CuA-Cytochrome c Domain from the Thermophilic Bacillus caa3-Type Cytochrome c Oxidase" @default.
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- W2032907492 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a021839" @default.
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