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Literature summary for 1.3.5.1 extracted from
- Computationally modeling mammalian succinate dehydrogenase kinetics identifies the origins and primary determinants of ROS production (2020), J. Biol. Chem., 295, 15262-15279 .
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| mitochondrial inner membrane | - |
Cavia porcellus | 5743 | - |
| mitochondrial inner membrane | - |
Bos taurus | 5743 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | within Fe-S clusters | Bos taurus |  |
| Fe2+ | within three Fe-S clusters | Cavia porcellus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| succinate + a quinone | Cavia porcellus | - |
fumarate + a quinol | - |
? | |
| succinate + a quinone | Bos taurus | - |
fumarate + a quinol | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | P31039 | - |
- |
| Cavia porcellus | H0VDG4 | - |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| heart | - |
Cavia porcellus | - |
| heart | - |
Bos taurus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| succinate + a quinone | - |
Cavia porcellus | fumarate + a quinol | - |
? | |
| succinate + a quinone | - |
Bos taurus | fumarate + a quinol | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| SDH | - |
Cavia porcellus |
| SDH | - |
Bos taurus |
| succinate dehydrogenase | - |
Cavia porcellus |
| succinate dehydrogenase | - |
Bos taurus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 37 | assay at | Cavia porcellus |
| 37 | - |
assay at | Bos taurus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
assay at | Bos taurus |
| 7.2 | 8 | assay at | Cavia porcellus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | bound in the SdhA subunit | Cavia porcellus | |
| FAD | bound in the SdhA subunit | Bos taurus | |
| Fe-S cluster | the SDHB subunit of the enzyme complex contains three iron-sulfur clusters (ISCs): [2Fe-2S], [4Fe-4S], and [3Fe-4S] | Cavia porcellus | |
| Fe-S cluster | the SDHB subunit of the enzyme complex contains three iron-sulfur clusters (ISCs): [2Fe-2S], [4Fe-4S], and [3Fe-4S] | Bos taurus | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | succinate dehydrogenase (SDH) can produce significant amounts of superoxide and hydrogen peroxide (H2O2), which hinders the development of next-generation antioxidant therapies targeting mitochondria | Cavia porcellus |
| additional information | succinate dehydrogenase (SDH) can produce significant amounts of superoxide and hydrogen peroxide (H2O2), which hinders the development of next-generation antioxidant therapies targeting mitochondria | Bos taurus |
| physiological function | succinate dehydrogenase (SDH) is an inner mitochondrial membrane protein complex that links the Krebs cycle to the electron transport system. It can produce significant amounts of superoxide and hydrogen peroxide (H2O2), kinetic mechanism and computational modelling including the major redox centers in the complex, namely FAD, three iron-sulfur clusters, and a transiently bound semiquinone, detailed overview. Oxidation state transitions involve a one- or two-electron redox reaction, each being thermodynamically constrained. When the quinone reductase site is inhibited or the quinone pool is highly reduced, superoxide is generated primarily by the FAD. In addition, H2O2 production is only significant when the enzyme is fully reduced, and fumarate is absent. SDH significantly contributes to total mitochondrial ROS production | Cavia porcellus |
| physiological function | succinate dehydrogenase (SDH) is an inner mitochondrial membrane protein complex that links the Krebs cycle to the electron transport system. It can produce significant amounts of superoxide and hydrogen peroxide (H2O2), kinetic mechanism and computational modelling including the major redox centers in the complex, namely FAD, three iron-sulfur clusters, and a transiently bound semiquinone, detailed overview. Oxidation state transitions involve a one- or two-electron redox reaction, each being thermodynamically constrained. When the quinone reductase site is inhibited or the quinone pool is highly reduced, superoxide is generated primarily by the FAD. In addition, H2O2 production is only significant when the enzyme is fully reduced, and fumarate is absent. SDH significantly contributes to total mitochondrial ROS production | Bos taurus |
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Release 2023.1 (January 2023)
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