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Protein sites of attack of N ‐chlorotaurine in Escherichia coli
Author(s) -
Arnitz Roland,
Sarg Bettina,
Ott Helmut W.,
Neher Andreas,
Lindner Herbert,
Nagl Markus
Publication year - 2006
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200500054
Subject(s) - escherichia coli , cysteine , biochemistry , chemistry , periplasmic space , incubation , bacteria , heat shock protein , biology , enzyme , genetics , gene
N ‐Chlorotaurine sodium (NCT) is a promising microbicidal agent for topical treatment of infections. Its targets of attack in Escherichia coli have been investigated by proteomics. Incubation in 1% NCT for 10 and 30 min revealed a change of the charge and a separation of numerous proteins into a series of spots with a different p I . Charge differences could be related to oxidation of cysteine residues to their corresponding sulfonic acids. Heat shock protein 60 appeared, while ribosome‐releasing factor, d‐ribose periplasmic binding protein, and malonyl‐CoA transacylase spots decreased. These results indicate penetration of oxidation capacity into the bacteria and destruction of essential proteins by NCT.