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Total synthesis of a simple metalloprotein-desulforedoxin.

Authors :
Tavares P
Wunderlich JK
Lloyd SG
LeGall J
Moura JJ
Moura I
Source :
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1995 Mar 17; Vol. 208 (2), pp. 680-7.
Publication Year :
1995

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 redox potential and spectroscopic properties (UV-Visible, EPR, Mössbauer).

Details

Language :
English
ISSN :
0006-291X
Volume :
208
Issue :
2
Database :
MEDLINE
Journal :
Biochemical and biophysical research communications
Publication Type :
Academic Journal
Accession number :
7695623
Full Text :
https://doi.org/10.1006/bbrc.1995.1392