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Molecular and catalytic properties of a peroxiredoxin–glutaredoxin hybrid from Neisseria meningitidis
Author(s) -
Rouhier Nicolas,
Jacquot Jean-Pierre
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01156-6
Subject(s) - glutaredoxin , neisseria meningitidis , peroxiredoxin , glutathione , chemistry , biochemistry , biology , enzyme , microbiology and biotechnology , bacteria , peroxidase , genetics
A hybrid protein from Neisseria meningitidis , which contains both a peroxiredoxin and a glutaredoxin domain, has been isolated. The enzyme was active in the reduction of various peroxides and dehydroascorbate in the presence of reduced glutathione. These findings suggest that both the peroxiredoxin and glutaredoxin domains are biochemically active in the fusion. Moreover, when expressed separately, the glutaredoxin domain was catalytically active and the peroxiredoxin domain possessed a weak activity when supplemented with exogenous glutaredoxin.