Architecture of succinate dehydrogenase and reactive oxygen species generation
| Autor: | Gary Cecchini, So Iwata, Susanna Törnroth, Bernadette Byrne, Rob Horsefield, César Luna-Chavez, Christophe Léger, Victoria Yankovskaya, Hideto Miyoshi |
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| Rok vydání: | 2003 |
| Předmět: |
Models
Molecular Cellular respiration Protein Conformation Ubiquinone Succinic Acid Heme Crystallography X-Ray Protein Structure Secondary Electron Transport chemistry.chemical_compound Multienzyme Complexes Superoxides Escherichia coli Anaerobiosis Flavin adenine dinucleotide chemistry.chemical_classification Reactive oxygen species Multidisciplinary Binding Sites biology Succinate dehydrogenase Electron Transport Complex II Fumarate reductase Electron transport chain Aerobiosis Protein Structure Tertiary Succinate Dehydrogenase Protein Subunits chemistry Biochemistry Mutation biology.protein Flavin-Adenine Dinucleotide Electron Transport Pathway Oxidoreductases Reactive Oxygen Species Oxidation-Reduction Dinitrophenols |
| Zdroj: | Science (New York, N.Y.). 299(5607) |
| ISSN: | 1095-9203 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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