Invitro mutated β subunits from the F1-ATPase of the thermophilic bacterium, PS3, containing glutamine in place of glutamic acid in positions 190 or 201 assembles with the α and γ subunits to produce inactive complexes-Reference-Cited by-同舟云学术

Invitro mutated β subunits from the F1-ATPase of the thermophilic bacterium, PS3, containing glutamine in place of glutamic acid in positions 190 or 201 assembles with the α and γ subunits to produce inactive complexes

Published:1987-07 Issue:2 Volume:146 Page:705-710
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Ohtsubo Michihiro,Yoshida Masasuke,Ohta Shigeo,Kagawa Yasuo,Yohda Masafumi,Date Takayasu

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference6 articles.

1. Reactivity of mitochondrial F1-ATPase to dicyclohexylcarbodiimide. Inactivation and binding studies

2. Identification of an essential glutamic acid residue in the beta subunit of the adenosine triphosphatase from the thermophilic bacterium PS3.

3. Inactivation of the bovine mitochondrial F1-ATPase with dicyclohexyl[14C]carbodiimide leads to the modification of a specific glutamic acid residue in the beta subunit.

4. The specificity of carboxyl group modification during the inactivation of the Escherichia coli F1-ATPase with dicyclohexyl[14C]carbodiimide.

5. Stable Structure of Thermophilic Proton ATPase Beta Subunit12

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