Redox Regulation of Mitochondrial ATP Synthase

Overview

Journal Trends Cardiovasc Med

Specialty Cardiology & Vascular Diseases

Date 2013 Jan 15

PMID 23312134

Citations 45

Authors

Sheng-Bing Wang

Christopher I Murray

Heaseung S Chung

Jennifer E Van Eyk

Affiliations

Soon will be listed here.

Abstract

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 F(1)F(0)-ATP synthase complex, and other matrix proteins/enzymes. Emerging evidence has linked Ox-PTMs 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 F(1)F(0)-ATP synthase complex is discussed in the context of heart failure and its possible clinical treatment.

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