Abstract
The primary structure of the 2Fe-2S ferredoxin from Halobacterium of the Dead Sea was determined and it consisted of 128 amino acid residues including an Nε{lunate}-acetyllysyl residue. Due to a high degree of sequence homology between this ferredoxin and the one from Halobacterium halobium, all tryptic peptides could be aligned in order. Only 20 amino acid differences were observed between these two halobacterial ferredoxins. The distribution of cysteinyl residues involved in the iron chelation was similar to that of chloroplast-type ferredoxins.
Original language | English |
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Pages (from-to) | 139-145 |
Number of pages | 7 |
Journal | BBA - Protein Structure |
Volume | 623 |
Issue number | 1 |
DOIs | |
State | Published - 29 May 1980 |
Externally published | Yes |
Keywords
- (Halobacterium, Dead Sea)
- Amino acid sequence
- Ferredoxin
- Iron-sulfur protein