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  • Title: Conversion of desulforedoxin into a rubredoxin center.
    Author: Yu L, Kennedy M, Czaja C, Tavares P, Moura JJ, Moura I, Rusnak F.
    Journal: Biochem Biophys Res Commun; 1997 Feb 24; 231(3):679-82. PubMed ID: 9070870.
    Abstract:
    Rubredoxin and desulforedoxin both contain an Fe(S-Cys)4 center. However, the spectroscopic properties of the center in desulforedoxin differ from rubredoxin. These differences arise from a distortion of the metal site hypothesized to result from adjacent cysteine residues in the primary sequence of desulforedoxin. Two desulforedoxin mutants were generated in which either a G or P-V were inserted between adjacent cysteines. Both mutants exhibited optical spectra with maxima at 278, 345, 380, 480, and 560 nm while the low temperature X-band EPR spectra indicated highspin Fe3+ ions with large rhombic distortions (E/D = 0.21-0.23). These spectroscopic properties are distinct from wild type desulforedoxin and virtually identical to rubredoxin.
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