Amino acid sequence of 2Fe-2S ferredoxin from an extreme halophile, Halobacterium of the dead sea

T. Hase, S. Wakabayashi, H. Matsubara, M. Mevarech, M. M. Werber

Research output: Contribution to journalArticlepeer-review

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 languageEnglish
Pages (from-to)139-145
Number of pages7
JournalBBA - Protein Structure
Volume623
Issue number1
DOIs
StatePublished - 29 May 1980
Externally publishedYes

Keywords

  • (Halobacterium, Dead Sea)
  • Amino acid sequence
  • Ferredoxin
  • Iron-sulfur protein

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