Blocking one non-catalytic ADP binding site results in complete inhibition of the F-type ATPase from the thermophilic Bacillus PS3

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Abstract

The F-type ATPase, TF0F1, from the thermophilic Bacillus PS3, which is free of nucleotides after isolation, was specifically loaded with one 2-azido ADP on a non-catalytic site. The enzyme was covalently modified to various extents and the rate of ATP synthesis and ATP hydrolysis was measured. Both ATP synthesis and ATP hydrolysis extrapolated to zero for covalentiy binding one nucleotide per enzyme. This was interpreted such that the non-catalytic sites are involved in the coupled catalytic process.

Original languageEnglish
Pages (from-to)141-144
Number of pages4
JournalBiochimica et Biophysica Acta: Bioenergetics
Volume1275
Issue number3
DOIs
Publication statusPublished - 31 Jul 1996
MoE publication typeNot Eligible

Keywords

  • 2-Azido nucleotide
  • Adenosine binding site
  • ATPase
  • ATPase TFF
  • F-type
  • H-
  • Thermophilic Bacillus PS3

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