Architecture of Succinate Dehydrogenase and Reactive Oxygen Species Generation

2003/01/30 by Victoria Yankovskaya, Rob Horsefield, Susanna Törnroth‐Horsefield +6 · 3 citations
Biochemistry, Genetics and Molecular Biology · #Mitochondrial Function and Pathology #Cancer, Hypoxia, and Metabolism #ATP Synthase and ATPases Research

paper · doi:10.1126/science.1079605

openalex publication_date 2003/01/30 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/25

Abstract

The structure of Escherichia coli succinate dehydrogenase (SQR), analogous to the mitochondrial respiratory complex II, has been determined, revealing the electron transport pathway from the electron donor, succinate, to the terminal electron acceptor, ubiquinone. It was found that the SQR redox centers are arranged in a manner that aids the prevention of reactive oxygen species (ROS) formation at the flavin adenine dinucleotide. This is likely to be the main reason SQR is expressed during aerobic respiration rather than the related enzyme fumarate reductase, which produces high levels of ROS. Furthermore, symptoms of genetic disorders associated with mitochondrial SQR mutations may be a result of ROS formation resulting from impaired electron transport in the enzyme.

Citations

• Natural engineering principles of electron tunnelling in biological oxidation–reduction

Cited by

• Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone pool
• Progress in understanding molecular mechanisms and evolution of resistance to succinate dehydrogenase inhibiting (SDHI) fungicides in phytopathogenic fungi
• Oxidative phosphorylation [wikipedia]