Theory of long binding events in single-molecule-controlled rotation experiments on F1-ATPase

Proc Natl Acad Sci U S A. 2017 Jul 11;114(28):7272-7277. doi: 10.1073/pnas.1705960114. Epub 2017 Jun 26.

Abstract

The theory of elastic group transfer for the binding and release rate constants for nucleotides in F1-ATPase as a function of the rotor angle is further extended in several respects. (i) A method is described for predicting the experimentally observed lifetime distribution of long binding events in the controlled rotation experiments by taking into account the hydrolysis and synthesis reactions occurring during these events. (ii) A method is also given for treating the long binding events in the experiments and obtaining the rate constants for the hydrolysis and synthesis reactions occurring during these events. (iii) The theory in the previous paper is given in a symmetric form, an extension that simplifies the application of the theory to experiments. It also includes a theory-based correction of the reported "on" and "off" rates by calculating the missed events. A near symmetry of the data about the angle of -40° and a "turnover" in the binding rate data vs. rotor angle for angles greater than [Formula: see text]40° is also discussed.

Keywords: F-ATPase; group transfer theory; hydrolysis; nucleotide binding; single-molecule imaging.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adenosine Diphosphate / chemistry*
  • Adenosine Triphosphate / chemistry
  • Hydrolysis
  • Ion Transport
  • Kinetics
  • Nucleotides / chemistry
  • Protein Binding
  • Proton-Translocating ATPases / chemistry*
  • Rotation

Substances

  • Nucleotides
  • Adenosine Diphosphate
  • Adenosine Triphosphate
  • Proton-Translocating ATPases