Unknown

Dataset Information

0

Oscillating Electric Field Measures the Rotation Rate in a Native Rotary Enzyme.


ABSTRACT: 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 mechanical modification of the enzyme, for the first time. The results suggest that a transmembrane AC field is able to synchronise the steps of ion-pumping in individual enzymes via a hold-and-release mechanism, which opens up the possibility of biotechnological exploitation. Our approach is likely to work for other transmembrane ion-transporting assemblies, not only rotary enzymes, to determine intrinsic in situ rates of ion pumping.

SUBMITTER: Ferencz CM 

PROVIDER: S-EPMC5366918 | biostudies-literature |

REPOSITORIES: biostudies-literature

Similar Datasets

| S-EPMC2951890 | biostudies-literature
| S-EPMC8595334 | biostudies-literature
| S-EPMC8747415 | biostudies-literature
| S-EPMC6200794 | biostudies-literature
| S-EPMC5056037 | biostudies-literature
| S-EPMC3102135 | biostudies-literature
| S-EPMC5104473 | biostudies-literature
| S-EPMC6265899 | biostudies-literature
| S-EPMC5064412 | biostudies-other
| S-EPMC6140629 | biostudies-literature