Identification of an essential lysine residue in the β subunit of the F1-ATPase from the thermophilic bacterium, PS3, using 7-chloro-4-nitro[14C]benzofurazan
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference27 articles.
1. The Mitochondrial ATPase. Evidence for a Single Essential Tyrosine Residue
2. Reactivity of the .beta. subunit of Escherichia coli adenosine triphosphatase with 4-chloro-7-nitrobenzofurazan
3. Reports of the 2nd European Bioenergetics Conference;Schafer,1982
4. Specific labelling of the (Ca2+ + Mg2+)-ATPase of Escherichia coli with 8-azido-ATP and 4-chloro-7-nitrobenzofurazan
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1. ATP Synthase and the Actions of Inhibitors Utilized To Study Its Roles in Human Health, Disease, and Other Scientific Areas;Microbiology and Molecular Biology Reviews;2008-12
2. Photoinactivation of the F1-ATPase from Spinach Chloroplasts by Dequalinium Is Accompanied by Derivatization of Methionine β183;Journal of Biological Chemistry;1997-12
3. The ATPase activity of the alpha 3 beta 3 complex of the F1-ATPase of the thermophilic bacterium PS3 is inactivated on modification of tyrosine 307 in a single beta subunit by 7-chloro-4-nitrobenzofurazan.;Journal of Biological Chemistry;1990-02
4. Selectivity of modification when latent and activated forms of the chloroplast F1-ATPase are inactivated by 7-chloro-4-nitrobenzofurazan;Archives of Biochemistry and Biophysics;1989-08
5. Mechanism of F1-ATPase studied by the genetic approach;Journal of Bioenergetics and Biomembranes;1988-08
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