Regulation of the F1F0-ATP synthase rotary nanomotor in its monomeric-bacterial and dimeric-mitochondrial forms.

ABSTRACT: The F(1)F(0)-adenosine triphosphate (ATP) synthase rotational motor synthesizes most of the ATP required for living from adenosine diphosphate, Pi, and a proton electrochemical gradient across energy-transducing membranes of bacteria, chloroplasts, and mitochondria. However, as a reversible nanomotor, it also hydrolyzes ATP during de-energized conditions in all energy-transducing systems. Thus, different subunits and mechanisms have emerged in nature to control the intrinsic rotation of the enzyme to favor the ATP synthase activity over its opposite and commonly wasteful ATPase turnover. Recent advances in the structural analysis of the bacterial and mitochondrial ATP synthases are summarized to review the distribution and mechanism of the subunits that are part of the central rotor and re

SUBMITTER: Garcia-Trejo JJ 

PROVIDER: S-EPMC2577739 | biostudies-literature | 2008 Apr

REPOSITORIES: biostudies-literature