Pulsed electron paramagnetic resonance studies of the interaction of magnesium-ATP and deuterium oxide with the iron protein of nitrogenase
- 1 March 1990
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 29 (12) , 3077-3082
- https://doi.org/10.1021/bi00464a026
Abstract
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 modulation 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.Keywords
This publication has 1 reference indexed in Scilit:
- The Coupling of Electron Transfer in Nitrogenase to the Hydrolysis of Magnesium Adenosine TriphosphateBiochemical Society Transactions, 1979