The Binding of Adenine Nucleotides to Apo-Electron-Transferring Flavoprotein1
| العنوان: | The Binding of Adenine Nucleotides to Apo-Electron-Transferring Flavoprotein1 |
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| المؤلفون: | Yasuzo Nishina, Kiyoshi Shiga, Kyosuke Sato |
| المصدر: | The Journal of Biochemistry. 112:804-810 |
| بيانات النشر: | Oxford University Press (OUP), 1992. |
| سنة النشر: | 1992 |
| مصطلحات موضوعية: | chemistry.chemical_classification, biology, Chemistry, Stereochemistry, food and beverages, Flavoprotein, Dehydrogenase, Riboflavin, General Medicine, Biochemistry, Electron-transferring flavoprotein, enzymes and coenzymes (carbohydrates), Enzyme, Adenine nucleotide, biology.protein, Nucleic acid, bacteria, heterocyclic compounds, Nucleotide, Molecular Biology |
| الوصف: | Apoprotein of electron-transferring flavoprotein (ETF) reacts with FAD as follows: A* A, A+FAD holoETF. Two different forms of apoETF (A* and A) convert into each other and only one of them, A, can associate with FAD [Sato, K. et al. (1991) J. Biochem. 109, 734-740]. In the present study, the reactions between apoETF and ATP, ADP, AMP, riboflavin, or FMN were investigated. It was revealed that all three adenine nucleotides bind with apoETF with the same kinetic reaction scheme as FAD, and compete with FAD. These results suggest that the nucleotides bind to A with the same location as the ADP part of FAD in holoETF and that the ADP-binding site of apoETF is generated upon conversion from A* to A. Neither riboflavin nor FMN bound to apoETF regardless of the presence or absence of the nucleotides, indicating that the ADP part of the FAD molecule is essential to the incorporation of the isoalloxazine ring into ETF. The binding rate constant of FAD to A was 1/20 of that of ADP while the dissociation rate constant was 1/1,000. This indicates that the riboflavin part of FAD inhibits the binding of FAD by steric hindrance, while after the binding, it stabilizes the complex. |
| تدمد: | 1756-2651 0021-924X |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_________::2896c26bbf8203cf48b05c09323b7cf1Test https://doi.org/10.1093/oxfordjournals.jbchem.a123980Test |
| رقم الانضمام: | edsair.doi...........2896c26bbf8203cf48b05c09323b7cf1 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 17562651 0021924X |
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