A mutational study of the energy transmission in E. coli ATP synthase

Abstract

ATP synthase catalyzes ATP synthesis by oxidative phosphorylation. With the unique mechanism and structure of ATP synthase, the energy transmission between the rotor and stator complex plays a vital role to maintain its proper function. Our previous study has discussed that upon γC87K mutation, a stronger interaction with βE381 could refrain the rotor complex from smooth spin, leading to insufficient energy coupling. In this study, we engineered alanine mutations to these residues to mimic a weaker rotor/stator interaction, and we found that multiple alanine mutation also impairs the enzyme performance. This research will add more pieces to understand the energy flow in ATP synthase.