Conversion of desulforedoxin into a rubredoxin center

Lian Yu, Matthew Kennedy, Christopher Czaja, Pedro Tavares, José J. G. Moura, Isabel Moura, Frank Rusnak

Research output: Contribution to journalArticlepeer-review

18 Citations (Scopus)

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 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.

Original languageEnglish
Pages (from-to)679-682
Number of pages4
JournalBiochemical And Biophysical Research Communications
Volume231
Issue number3
DOIs
Publication statusPublished - 24 Feb 1997

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