Redox Regulation of Mitochondrial ATP Synthase

Reversible cysteine oxidative post-translational modifications (Ox-PTMs) represent an important mechanism to regulate protein structure and function. In mitochondria, redox reactions can modulate components of the electron transport chain (ETC), the F1F0-ATP synthase complex, and other matrix proteins/enzymes. Emerging evidence has linked Ox-FTMs to mitochondrial dysfunction and heart failure, highlighting some potential therapeutic avenues. Ox-PTMs can modify a variety of amino acid residues, including cysteine, and have the potential to modulate the function of a large number of proteins. Among this group, there is a selected subset of amino acid residues that can function as redox switches. These unique sites are proposed to monitor the cell's oxidative balance through their response to the various Ox-PTMs. In this review, the role of Ox-PTMs in the regulation of the F1F0-ATP synthase complex is discussed in the context of heart failure and its possible clinical treatment. (Trends Cardiovasc Med 23:14-18) (C) 2013 Elsevier Inc. All rights reserved.