Unusual pKa of the carboxylate at the putative catalytic position of the thermophilic F1-ATPase beta subunit determined by 13C-NMR

FEBS Letters
K TozawaH Akutsu

Abstract

Glutamic acid-190 in the beta subunit of F1-ATPase from thermophilic Bacillus PS-3 (TF1) was reported to be essential for the ATPase activity. The mutant TF1beta subunit in which Glu-190 had been substituted by cysteine was carboxymethylated with 13C-labeled monoiodoacetic acid. The pKa value of the carboxymethylene group at the 190 position was determined as 5.6 +/- 0.4 by 13C-NMR. On the basis of this value, the pKa of the carboxylate of Glu-190 of the TF1beta subunit was estimated to be 6.8 +/- 0.5. The unusually high pKa could play a role in the catalytic mechanism of F1-ATPase.

References

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Citations

Aug 18, 2005·Proceedings of the National Academy of Sciences of the United States of America·Daniel W SchuerchRodney K Tweten
Sep 9, 2011·Journal of the American Chemical Society·Andras LukacsPeter J Tonge
Feb 6, 2020·The Journal of Biological Chemistry·Warintra PitsawongAnne-Frances Miller
Oct 13, 2017·Proceedings of the Japan Academy. Series B, Physical and Biological Sciences·Hideo Akutsu
Dec 6, 1997·Biochemical and Biophysical Research Communications·Y Kagawa, T Hamamoto
Aug 27, 1999·Advances in Biophysics·Y Kagawa
Aug 13, 2011·Biochimica Et Biophysica Acta·Eileen M Hotze, Rodney K Tweten

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