TY - JOUR
T1 - IF1
T2 - setting the pace of the F1Fo-ATP synthase
AU - Campanella, Michelangelo
AU - Parker, Nadeene
AU - Tan, Choon Hong
AU - Hall, Andrew M.
AU - Duchen, Michael R.
PY - 2009/7
Y1 - 2009/7
N2 - When mitochondrial function is compromised and the mitochondrial membrane potential (Δψm) falls below a threshold, the F1Fo-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 IF1, an endogenous F1Fo-ATPase inhibitor. IF1, therefore, preserves ATP at the expense of Δψm. Despite a wealth of detailed knowledge on the biochemistry of the interaction of IF1 and the F1Fo-ATPase, little is known about its physiological activity. Emerging research suggests that IF1 has a wider ranging impact on mitochondrial structure and function than previously thought.
AB - When mitochondrial function is compromised and the mitochondrial membrane potential (Δψm) falls below a threshold, the F1Fo-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 IF1, an endogenous F1Fo-ATPase inhibitor. IF1, therefore, preserves ATP at the expense of Δψm. Despite a wealth of detailed knowledge on the biochemistry of the interaction of IF1 and the F1Fo-ATPase, little is known about its physiological activity. Emerging research suggests that IF1 has a wider ranging impact on mitochondrial structure and function than previously thought.
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U2 - 10.1016/j.tibs.2009.03.006
DO - 10.1016/j.tibs.2009.03.006
M3 - Article
C2 - 19559621
AN - SCOPUS:67649948810
VL - 34
SP - 343
EP - 350
JO - Trends in Biochemical Sciences
JF - Trends in Biochemical Sciences
SN - 0376-5067
IS - 7
ER -