Cookies help us deliver our services. By using our services, you agree to our use of cookies. More information

Campanella 2009 Trends Biochem Sci

From Bioblast
Publications in the MiPMap
Campanella M, Parker N, Choon Hong Tan, Hall AM, Duchen MR (2009) IF(1): setting the pace of the F(1)F(o)-ATP synthase. Trends Biochem Sci 34:343-50.

ยป PMID:19559621 Open Access

Campanella M, Parker N, Choon Hong Tan, Hall AM, Duchen MR (2009) Trends Biochem Sci

Abstract: When mitochondrial function is compromised and the mitochondrial membrane potential (Deltapsi(m)) falls below a threshold, the F(1)F(o)-ATP synthase can reverse, hydrolysing ATP to pump protons out of the mitochondrial matrix. Although this activity can deplete ATP and precipitate cell death, it is limited by the mitochondrial protein IF(1), an endogenous F(1)F(o)-ATPase inhibitor. IF(1), therefore, preserves ATP at the expense of Deltapsi(m). Despite a wealth of detailed knowledge on the biochemistry of the interaction of IF(1) and the F(1)F(o)-ATPase, little is known about its physiological activity. Emerging research suggests that IF(1) has a wider ranging impact on mitochondrial structure and function than previously thought.

Cited by

  • Komlรณdi et al (2022) The protonmotive force - not merely membrane potential. MitoFit Preprints 2022 (in prep)

Labels:






MitoFit 2022 pmF