Chicken mitochondrial cytochrome C oxidase subunit II: comparative analysis among the vertebrates.
The chicken cytochrome c oxidase subunit II (COII) was cloned and sequenced. A comparison 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.
Lee
Y H
YH
Institute of Biochemistry, National Yang-Ming Medical College, Taipei, Taiwan, Republic of China.
Liaw
L L
LL
Tsai
T Y
TY
Wei
Y H
YH
Lo
S J
SJ
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D002645:Chickens; D003001:Cloning, Molecular; D003062:Codon; D003576:Electron Transport Complex IV / Q000235:genetics*; D005796:Genes; D006801:Humans; D051379:Mice; D008928:Mitochondria / Q000201:enzymology*; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D014981:Xenopus
D003062:Codon; D003576:Electron Transport Complex IV