PMID: 8597569Feb 8, 1996Paper

Histidine-49 is necessary for the pH-dependent transition between active and inactive states of the bovine F1-ATPase inhibitor protein

Biochimica Et Biophysica Acta
R A SchnizerS M Schuster

Abstract

The role of the histidyl residue at position 49 (H49) of the bovine mitochondrial F1-ATPase inhibitor protein (F1I) was examined by site-directed mutagenesis. Six amino acids (Q, E, K, V, L, and I) were substituted for H49 and the activities of the resulting inhibitor proteins were characterized with respect to pH. Each of the six mutations abolished the pH sensitivity which is characteristic of wild-type F1I. At pH 8.0 each of the mutations caused an increase in apparent maximum inhibition and a decrease in apparent Ki relative to wild type. At pH 6.7 the hydrophilic substitutions had little effect on apparent Ki, while the hydrophobic substitutions caused increases of 3.5- to 8.5-fold relative to wild type. The ratios of apparent Ki at pH 8.0 to apparent Ki at pH 6.7 were in the range of 0.5 to 1.6 for the mutants, whereas the wild-type value is 15.0. The mutations appear to shift the equilibrium between active and inactive conformations of F1I toward the active state. We find that H49 is required by F1I for sensitivity to pH and that it may facilitate the transition between active and inactive states of F1I. A possible role for H49 in the stabilization of the inactive state through participation in a multivalent complex with...Continue Reading

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Citations

Feb 16, 2016·Biochimica Et Biophysica Acta·Javier García-Bermúdez, José M Cuezva
Jun 6, 2000·Biochimica Et Biophysica Acta·D W Green, G J Grover
Apr 2, 2014·Biochimica Et Biophysica Acta·Inmaculada Martínez-Reyes, José M Cuezva
Feb 9, 2000·Bioscience, Biotechnology, and Biochemistry·N IchikawaY Masazumi
Jun 1, 2000·The Journal of Biological Chemistry·E CabezonJ E Walker
May 9, 2019·Proceedings of the National Academy of Sciences of the United States of America·Vytaute BoreikaiteJohn E Walker

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