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Conversion of desulforedoxin into a rubredoxin center.

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Yu L,Kennedy M,Czaja C,Tavares P,Moura JJ,Moura I,Rusnak F

doi

10.1006/bbrc.1997.6171

subject

Has Abstract

pub_date

1997-02-24 00:00:00

pages

679-82

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(97)96171-4

journal_volume

231

pub_type

杂志文章

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