Linking structural features from mitochondrial and bacterial F-type ATP synthases to their distinct mechanisms of ATPase inhibition. Issue 1 (October 2015)

• Record Type: Journal Article
• Authors: Krah, Alexander
• Is Part Of: Progress in biophysics and molecular biology. Volume 119:Issue 1(2015)
• Page Start: 94
• Page End: 102
• Publication Date: 2015-10
• Subjects: F-type ATP synthase -- F1-domain -- IF1-inhibition -- ε inhibition; Biophysics -- Periodicals; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular Biology -- Periodicals; Biophysique -- Périodiques; Biochimie -- Périodiques; 571.4
• DOI: 10.1016/j.pbiomolbio.2015.06.005
• Languages: English
• ISSNs: 0079-6107

Abstract

Abstract: 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 Fo domain, namely the c-ring, causing a conformational change in the soluble F1 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 ε and ζ) F-type ATP synthases, based on available structural, biophysical and biochemical data.