Ontology highlight
ABSTRACT:
SUBMITTER: Ferencz CM
PROVIDER: S-EPMC5366918 | biostudies-literature | 2017 Mar
REPOSITORIES: biostudies-literature
Ferencz Csilla-Maria CM Petrovszki Pál P Dér András A Sebők-Nagy Krisztina K Kóta Zoltán Z Páli Tibor T
Scientific reports 20170327
Rotary enzymes are complex, highly challenging biomolecular machines whose biochemical working mechanism involves intersubunit rotation. The true intrinsic rate of rotation of any rotary enzyme is not known in a native, unmodified state. Here we use the effect of an oscillating electric (AC) field on the biochemical activity of a rotary enzyme, the vacuolar proton-ATPase (V-ATPase), to directly measure its mean rate of rotation in its native membrane environment, without any genetic, chemical or ...[more]