Abstract
The chicken cytochrome c oxidase subunit II (COII) was cloned and sequenced. A comparision of the deduced chicken COII sequence with 4 other vertebrate counterparts revealed 64-66% amino acid sequence homology and 68-70% nucleotide sequence homology. Four peptide segments each of nine amino acids long are highly conserved across the 5 species. A redox-center was formed by three of these highly conserved domains, which include two invariant Cys and two invariant His residues for copper ion coordination, three strictly conserved Glu or Asp residues for cytochrome c binding, and highly conserved aromatic acid residues for electron transfer.
| Original language | English |
|---|---|
| Pages (from-to) | 889-898 |
| Number of pages | 10 |
| Journal | Biochemistry international |
| Volume | 19 |
| Issue number | 4 |
| State | Published - Oct 1989 |