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A fourth subunit is present in cytochrome c oxidase from the thermophilic bacterium PS3
Author(s) -
Sone Nobuhito,
Shimada Shin-ichi,
Ohmori Tamiya,
Souma Yukiko,
Gonda Masahiro,
Ishizuka Mono
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80202-t
Subject(s) - protein subunit , cytochrome c oxidase , oxidase test , biochemistry , open reading frame , thermophile , cytochrome , escherichia coli , peptide sequence , cytochrome c , biology , cytochrome b , methionine , amino acid , microbiology and biotechnology , chemistry , gene , enzyme , mitochondrion , mitochondrial dna
A new putative subunit was found in cytochrome c oxidase ( aa 3 ‐type) of the thermophilic bacterium PS3. The N‐terminal amino acid sequence of this12 kDa protein coincides with the deduced sequence of an open reading frame found downstream from the gene encoding subunit I of the PS3 cytochrome oxidase [(1988) J. Biochem. 103, 606‐610]. This small hydrophobic protein, composed of 109 amino acid residues after the initial methionine residue has been processed, shows homology with the subunit IV ( cyoD product) of cytochrome bo ‐type quinol oxidase of Escherichia coli .