Conversion of desulforedoxin into a rubredoxin center.
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.
Yu
L
L
Section of Hematology Research, Mayo Clinic and Foundation, Rochester, Minnesota 55905, USA.
Kennedy
M
M
Czaja
C
C
Tavares
P
P
Moura
J J
JJ
Moura
I
I
Rusnak
F
F
D003545:Cysteine / Q000737:chemistry; D003901:Desulfovibrio / Q000737:chemistry; D004578:Electron Spin Resonance Spectroscopy; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D013058:Mass Spectrometry; D016297:Mutagenesis, Site-Directed; D012416:Rubredoxins / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet
D007506:Iron-Sulfur Proteins; D012416:Rubredoxins; C022220:desulforedoxin; D003545:Cysteine