Replacement of arginine 246 by histidine in the beta subunit of Escherichia coli H+-ATPase resulted in loss of multi-site ATPase activity.
Open Access
- 1 July 1986
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 261 (20) , 9196-9201
- https://doi.org/10.1016/s0021-9258(18)67638-0
Abstract
No abstract availableThis publication has 50 references indexed in Scilit:
- Rhodopseudomonas blastica atp operonJournal of Molecular Biology, 1984
- The UNC operon nucleotide sequence, regulation and structure of ATP-synthaseBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1984
- Defective proton ATPase of uncA mutants of Escherichia coli. 5'-adenylyl 5'-imidodiphosphate binding and ATP hydrolysisBiochemistry, 1984
- STRUCTURE AND FUNCTION OF H+‐ATPase: WHAT WE HAVE LEARNED FROM Escherichia coli H+‐ATPase*Annals of the New York Academy of Sciences, 1982
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982
- Nucleotide sequence of the genes for β and ε subunits of proton-translocating ATPase from Escherichia coliBiochemical and Biophysical Research Communications, 1982
- Functional groups at the catalytic site of BF1 adenosine triphosphatase from E. coliBiochemistry, 1982
- Nucleotide sequence of the genes coding for α, β and γ subunits of the proton-translocating ATPase ofBiochemical and Biophysical Research Communications, 1981
- 4-Azido-2-nitrophenyl phosphate, a new photoaffinity derivative of inorganic phosphate. Study of its interaction with the inorganic phosphate binding site of beef heart mitochondrial adenosine triphosphataseBiochemistry, 1980
- Reconstitution of ATPase activity from the isolated α, β, and γ subunits of the coupling factor, F1, of Escherichia coliBiochemical and Biophysical Research Communications, 1977