Journal
PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY
Volume 119, Issue 1, Pages 94-102Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.pbiomolbio.2015.06.005
Keywords
F-type ATP synthase; F-1-domain; IF1-inhibition; epsilon inhibition
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Funding
- Japan Society for the Promotion of Science (JSPS) [P13705]
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ATP synthases are molecular motors, which synthesize ATP, the ubiquitous energy source in all living cells. They use an electrochemical gradient to drive a rotation in the membrane embedded F-0 domain, namely the c-ring, causing a conformational change in the soluble F-1 domain which leads to the catalytic event. In the opposite fashion, they can also hydrolyse ATP to maintain the ion gradient across the membrane. To prevent wasteful ATP hydrolysis, bacteria and mammals have developed peculiar mechanistic features in addition to a common one, namely MgADP inhibition. Here I discuss the distinct ATPase inhibition mechanism in mitochondrial (IF1) and bacterial (subunits epsilon and zeta) F-type ATP synthases, based on available structural, biophysical and biochemical data. (C) 2015 Elsevier Ltd. All rights reserved.
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