Total synthesis of a simple metalloprotein - Desulforedoxin

Pedro Tavares, John K. Wunderlich, Steven G. Lloyd, Jean LeGall, José J. G. Moura, Isabel Moura

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Desulforedoxin is a protein purified from cellular extracts of Desulfovibrio gigas. It is a small (7.9 kDa) dimeric protein that contains a distorted rubredoxin like center (one single iron coordinated by four cysteinyl residues). Due to the simplicity of the polypeptide chain and of the iron center, an attempt was made to chemically produce this protein. A 36 amino acid polypeptide chain was synthesized based on the known sequence of native Desulforedoxin. The iron center was then reconstituted and the biochemical and spectroscopic characteristics of this synthetic protein were investigated. The final product has an equal sequence to the protein purified from D. gigas. The synthetic and natural Dx are very similar, in terms of redox potential and spectroscopic properties (UV-Visible, EPR, Mossbauer).

Original languageEnglish
Pages (from-to)680-687
Number of pages8
JournalBiochemical And Biophysical Research Communications
Volume208
Issue number2
DOIs
Publication statusPublished - 1 Jan 1995

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