Chicken mitochondrial cytochrome C oxidase subunit II: Comparative analysis among the vertebrates

Y. H. Wu Lee, L. L. Liaw, T. Y. Tsai, Y. H. Wei, S. J. Lo

Research output: Contribution to journalJournal Article peer-review

1 Scopus citations

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 languageEnglish
Pages (from-to)889-898
Number of pages10
JournalBiochemistry International
Volume19
Issue number4
StatePublished - 1989
Externally publishedYes

Fingerprint

Dive into the research topics of 'Chicken mitochondrial cytochrome C oxidase subunit II: Comparative analysis among the vertebrates'. Together they form a unique fingerprint.

Cite this