Pulsed electron paramagnetic resonance studies of the interaction of magnesium-ATP and deuterium oxide with the iron protein of nitrogenase
| العنوان: | Pulsed electron paramagnetic resonance studies of the interaction of magnesium-ATP and deuterium oxide with the iron protein of nitrogenase |
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| المؤلفون: | W. B. Mims, Jack Peisach, L. E. Mortenson, John McCracken, William H. Orme-Johnson, T. V. Morgan |
| المصدر: | Biochemistry. 29:3077-3082 |
| بيانات النشر: | American Chemical Society (ACS), 1990. |
| سنة النشر: | 1990 |
| مصطلحات موضوعية: | chemistry.chemical_classification, Chemistry, Pulsed EPR, Nitrogenase, Resonance, Biochemistry, law.invention, Nuclear magnetic resonance, Deuterium, law, Electric field, Spin echo, Metalloprotein, Electron paramagnetic resonance |
| الوصف: | Mg-ATP binds to the iron protein component of nitrogenase. The magnetic field dependence of the linear electric field effect (LEFE) in pulsed EPR is consistent with a single 4Fe-4S cluster. The LEFE is virtually unaltered when Mg-ATP is bound. Electron spin echo envelope modulation techniques were employed to evaluate the possibility of a magnetic interaction between 31P of Mg-ATP and the Fe-S center of the iron protein. None was detected. However, weak modulations possibly attributable to peptide 14N were seen, and these were slightly shifted by Mg-ATP addition. Further, protons in the vicinity of the Fe-S cluster of the protein readily exchange with D2O, and this process is unaffected by Mg-ATP. |
| تدمد: | 1520-4995 0006-2960 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_________::f4f3a495755569481467b6df4ad8d92f https://doi.org/10.1021/bi00464a026 |
| رقم الأكسشن: | edsair.doi...........f4f3a495755569481467b6df4ad8d92f |
| قاعدة البيانات: | OpenAIRE |
Find this issue from the American Chemical Society | تدمد: | 15204995 00062960 |
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