Pulsed electron paramagnetic resonance studies of the interaction of Mg-ATP and D2O with the iron protein of nitrogenase

Autor: T V, Morgan, J, McCracken, W H, Orme-Johnson, W B, Mims, L E, Mortenson, J, Peisach
Rok vydání: 1990
Předmět:
Zdroj: Biochemistry. 29(12)
ISSN: 0006-2960
Popis: 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.
Databáze: OpenAIRE