@article {5376,
	title = {Conversion of desulforedoxin into a rubredoxin center},
	journal = {Biochemical And Biophysical Research Communications},
	volume = {{231}},
	number = {{3}},
	year = {1997},
	note = {n/a},
	pages = {{679-682}},
	abstract = {<p>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 high-spin 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. (C) 1997 Academic Press.</p>
},
	author = {Yu, L. and Kennedy, M. and Czaja, C. and Tavares, P and Moura, J. J. G. and Moura, I. and Rusnak, F.}
}
