The 2-Oxoacid Dehydrogenase Complexes in Mitochondria Can Produce Superoxide/Hydrogen Peroxide at Much Higher Rates Than Complex I

• Published in: The Journal of biological chemistry Vol. 289; no. 12; pp. 8312 - 8325
• Main Authors: Quinlan, Casey L., Goncalves, Renata L.S., Hey-Mogensen, Martin, Yadava, Nagendra, Bunik, Victoria I., Brand, Martin D.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 21.03.2014; American Society for Biochemistry and Molecular Biology
• Subjects: 2-Oxoglutarate Dehydrogenase Complex; Animals; Bioenergetics; Branched-chain 2-Oxoacid Dehydrogenase Complex; Branched-chain Ketoacid Dehydrogenase; Female; Hydrogen Peroxide - metabolism; Ketoglutarate Dehydrogenase Complex - metabolism; Mitochondria; Mitochondria, Muscle - enzymology; Mitochondria, Muscle - metabolism; Muscle, Skeletal - enzymology; Muscle, Skeletal - metabolism; NAD - metabolism; NADH Autofluorescence; Oxidation-Reduction; Pyruvate Dehydrogenase Complex; Pyruvate Dehydrogenase Complex - metabolism; Rat; Rats; Rats, Wistar; Reactive Oxygen Species (ROS); Skeletal Muscle; Superoxides - metabolism; α-Ketoglutarate Dehydrogenase; Branched-chain Ketoacid Dehydrogenase; Mitochondria; Pyruvate Dehydrogenase Complex; Reactive Oxygen Species (ROS); Skeletal Muscle; 2-Oxoglutarate Dehydrogenase Complex; Rat; NADH Autofluorescence; α-Ketoglutarate Dehydrogenase; Branched-chain 2-Oxoacid Dehydrogenase Complex

Several flavin-dependent enzymes of the mitochondrial matrix utilize NAD+ or NADH at about the same operating redox potential as the NADH/NAD+ pool and comprise the NADH/NAD+ isopotential enzyme group. Complex I (specifically the flavin, site IF) is often regarded as the major source of matrix super...