AROMATIC RINGS OF TYROSINE RESIDUES AT ADENINE-NUCLEOTIDE BINDING-SITES OF THE BETA-SUBUNITS OF F1-ATPASE ARE NOT NECESSARY FOR ATPASE ACTIVITY

Using site-directed mutagenesis, Tyr-307, Tyr-341, or Tyr-364, supposedly located at the adenine nucleotide binding site(s) of the β subunits of F1-ATPase from the thermophilic bacterium PS3, was replaced with Phe or Cys. The α3β3 complexes reconstituted from the α subunits and individual mutant β subunits hydrolyzed ATP. Thus, neither the hydroxyl groups nor the aromatic rings in these positions are required for ATPase activity of F1-ATPase. © 1990.