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Calculation of Cys 30 ΔpK a 's and oxidising power for DsbA mutants
Author(s) -
Warwicker J.,
Gane P.J.
Publication year - 1996
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 - 10.1016/0014-5793(96)00358-4
Subject(s) - dsba , thioredoxin , chemistry , redox , cysteine , mutant , amino acid , active site , oxidizing agent , biochemistry , inorganic chemistry , organic chemistry , enzyme , escherichia coli , periplasmic space , gene
DsbA possesses a redox active disulphide, with the equilibrium strongly shifted towards the reduced form as compared to its structural homologue, thioredoxin. It is widely believed that the two amino acids that separate the active site cysteines play a crucial role in determining oxidising power within the thioredoxin family. Data concerning redox and pK a properties for DsbA mutants in this region are available. Electrostatics calculations show reasonable agreement with the experimental data, and support the suggestion that amino acids outside of the CXXC active site sequence are as important in determining oxidising power within the thioredoxin family as are those within it.