Total synthesis of a simple metalloprotein-desulforedoxin.
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).
Tavares
P
P
Departamento de Química e Centro de Química Fina e Biotecnologia, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, Monte de Caparica, Portugal.
Wunderlich
J K
JK
Lloyd
S G
SG
LeGall
J
J
Moura
J J
JJ
Moura
I
I
D003545:Cysteine / Q000737:chemistry; D003901:Desulfovibrio / Q000737:chemistry; D004578:Electron Spin Resonance Spectroscopy; D007506:Iron-Sulfur Proteins / Q000138:chemical synthesis*; D013056:Spectrophotometry, Ultraviolet; D013057:Spectrum Analysis
D007506:Iron-Sulfur Proteins; C022220:desulforedoxin; D003545:Cysteine