Structural Basis for Malfunction in Complex II

• Published in: The Journal of biological chemistry Vol. 287; no. 42; pp. 35430 - 35438
• Main Authors: Iverson, Tina M., Maklashina, Elena, Cecchini, Gary
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 12.10.2012; American Society for Biochemistry and Molecular Biology
• Subjects: Adenosine Triphosphate - biosynthesis; Animals; Citric Acid Cycle - physiology; Electron Transport; Electron Transport Complex II - physiology; Escherichia coli - enzymology; Escherichia coli Proteins - metabolism; Humans; Membrane Enzymes; Metabolic Diseases; Minireviews; Mitochondria; Phosphorylation - physiology; Respiration; Structure-Activity Relationship; Tricarboxylic Acid (TCA) Cycle; Tumor Metabolism; Tumor Metabolism; Electron Transport; Mitochondria; Membrane Enzymes; Metabolic Diseases; Respiration; Tricarboxylic Acid (TCA) Cycle
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.R112.408419

Complex II couples oxidoreduction of succinate and fumarate at one active site with that of quinol/quinone at a second distinct active site over 40 Å away. This process links the Krebs cycle to oxidative phosphorylation and ATP synthesis. The pathogenic mutation or inhibition of human complex II or its assembly factors is often associated with neurodegeneration or tumor formation in tissues derived from the neural crest. This brief overview of complex II correlates the clinical presentations of a large number of symptom-associated alterations in human complex II activity and assembly with the biochemical manifestations of similar alterations in the complex II homologs from Escherichia coli. These analyses provide clues to the molecular basis for diseases associated with aberrant complex II function.