Flexibility and dynamics of NhaA Na +/H +-antiporter of Escherichia coli studied by Fourier transform infrared spectroscopy

NhaA (41,355 Da) is a Na +/H + antiporter of Escherichia coli which plays a central role in regulation of intracellular pH, cellular Na + content, and cell volume [E. Padan, S. Schuldiner, J. Exp. Biol. 196 (1994) 443]. Its activity is strongly regulated by pH and increases over 3 orders of magnitud...

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Published in:Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy Molecular and biomolecular spectroscopy, 2009-02, Vol.72 (1), p.102-109
Main Authors: Džafić, E., Klein, O., Screpanti, E., Hunte, C., Mäntele, W.
Format: Article
Language:English
Subjects:
1H/ 2H exchange
ATR spectroscopy
Deuterium
Escherichia coli
Escherichia coli - metabolism
Escherichia coli NhaA
Escherichia coli Proteins - chemistry
FTIR spectroscopy
Microdialysis
Mutant Proteins - chemistry
Na +/H + antiporter
Perfusion cell
Pliability
Protein accessibility
Protein Structure, Secondary
Protons
Sodium-Hydrogen Exchangers - chemistry
Spectroscopy, Fourier Transform Infrared
Temperature
Thermal stability
Time Factors
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Summary:NhaA (41,355 Da) is a Na +/H + antiporter of Escherichia coli which plays a central role in regulation of intracellular pH, cellular Na + content, and cell volume [E. Padan, S. Schuldiner, J. Exp. Biol. 196 (1994) 443]. Its activity is strongly regulated by pH and increases over 3 orders of magnitude between pH 7 and 8 [A. Rothman, Y. Gerchman, E. Padan, S. Schuldiner, Biochemistry 36 (1997) 14572]. Protein dynamics and flexibility in the activated and inactivated state, respectively, was analysed by probing accessibility in 1H/ 2H exchange experiments for the wild type and the mutant G338S which is constitutively active independent of pH [A. Rimon, Y. Gerchman, Z. Kariv, E. Padan, J. Biol. Chem. 273 (1998) 26470]. This was studied by ATR–FTIR difference spectroscopy using a home built microvolume (
ISSN:1386-1425
DOI:10.1016/j.saa.2008.08.015