The structural gene coding for cytochrome b-562 isolated from the cytochrome b-c1 complex of Rhodobacter (Rhodopseudomonas) sphaeroides has been cloned. Its nucleotide sequence has been determined and the amino acid sequence was deduced therefrom. It consists of 157 amino acids Mr 17,237) and contains four hydro-phobic segments. The first 30 residues in the predicted amino acid sequence are the same as those determined for the NH2,-terminal portion of purified cytochrome b-562. The amino acid composition is in accord with that determined for the pure protein. From the hydropathy profile and molar ratio of protoheme to cytochrome b-562, it is suggested that the structural and functional unit of the cytochrome is a two-heme cross-linked homodimer.
|Number of pages||8|
|Journal||Journal of biochemistry|
|Publication status||Published - Dec 1987|
All Science Journal Classification (ASJC) codes
- Molecular Biology