title: Mitochondrial respiratory chain complexes as sources and targets of thiol-based redox-regulation.
abstract: The respiratory chain of the inner mitochondrial membrane is a unique assembly of protein complexes that transfers the electrons of reducing equivalents extracted from foodstuff to molecular oxygen to generate a proton-motive force as the primary energy source for cellular ATP-synthesis. Recent evidence indicates that redox reactions are also involved in regulating mitochondrial function via redox-modification of specific cysteine-thiol groups in subunits of respiratory chain complexes. Vice versa the generation of reactive oxygen species (ROS) by respiratory chain complexes may have an impact on the mitochondrial redox balance through reversible and irreversible thiol-modification of specific target proteins involved in redox signaling, but also pathophysiological processes. Recent evidence indicates that thiol-based redox regulation of the respiratory chain activity and especially S-nitrosylation of complex I could be a strategy to prevent elevated ROS production, oxidative damage and tissue necrosis during ischemia-reperfusion injury. This review focuses on the thiol-based redox processes involving the respiratory chain as a source as well as a target, including a general overview on mitochondria as highly compartmentalized redox organelles and on methods to investigate the redox state of mitochondrial proteins. This article is part of a Special Issue entitled: Thiol-Based Redox Processes.
authors.affiliation: Clinic of Anesthesiology, Intensive-Care Medicine and Pain Therapy, University Hospital Frankfurt, 60590 Frankfurt am Main, Germany.
authors.forename: Stefan
authors.initials: S
authors.lastname: Dröse
authors.affiliation: Radboud University Medical Centre, Nijmegen Centre for Mitochondrial Disorders, Geert Grooteplein-Zuid 10, 6525 GA Nijmegen, The Netherlands; Cluster of Excellence "Macromolecular Complexes", Goethe-University, Frankfurt am Main, Germany. Electronic address: ulrich.brandt@radboudumc.nl.
authors.forename: Ulrich
authors.initials: U
authors.lastname: Brandt
authors.affiliation: Functional Proteomics, SFB 815 Core Unit, Faculty of Medicine, Johann Wolfgang Goethe University, 60590 Frankfurt am Main, Germany; Cluster of Excellence "Macromolecular Complexes", Goethe-University, Frankfurt am Main, Germany.
authors.forename: Ilka
authors.initials: I
authors.lastname: Wittig
mesh_terms: D000818:Animals; D004579:Electron Transport; D042967:Electron Transport Complex I / Q000378:metabolism*; D006801:Humans; D008928:Mitochondria / Q000378:metabolism*; D024101:Mitochondrial Proteins; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D017382:Reactive Oxygen Species / Q000378:metabolism*; D013438:Sulfhydryl Compounds / Q000737:chemistry*
chemical_list: D024101:Mitochondrial Proteins; D017382:Reactive Oxygen Species; D013438:Sulfhydryl Compounds; D042967:Electron Transport Complex I
keywords: Active/deactive transition; Mitochondria; Reactive oxygen species (ROS); Redox proteomics; Respiratory chain complex; S-nitrosylation