Mn-Mn interaction in adenylylated and unadenylylated glutamine synthetase.
The distance between the two catalytically important metal ions of glutamine synthetase was determined by electron paramagnetic resonance (EPR). Mn(II) binds more tightly to the n1 site of this enzyme in the presence of methionine sulfoximine and the influence of Mn(II) bound at the n2 site on the EPR spectrum of Mn(II) at n1 was studied. A monotonic increase in the EPR spectrum of Mn(II) was observed at Mn:E (subunit) ratios of 0 to 0.8. After this point as Mn(II) was added to about 1.8 Mn:E, a decrease in the EPR signal was observed. This phenomenon was found for both adenylylated and unadenylylated forms of glutamine synthetase. The data were analyzed using a theory for dipolar electron-electron relaxation and a distance of 10-12 A was computed for the Mn(II)-Mn(II) separation. These data demonstrate that both modified and unmodified forms of glutamine synthetase which have different catalytic activities have a similar spatial relationship between the two catalytic metal ion sites.
D000249:Adenosine Monophosphate / Q000378:metabolism*; D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D004578:Electron Spin Resonance Spectroscopy; D004926:Escherichia coli / Q000201:enzymology; D005974:Glutamate-Ammonia Ligase / Q000378:metabolism*; D008345:Manganese / Q000378:metabolism*; D008433:Mathematics; D011485:Protein Binding
D000249:Adenosine Monophosphate; D008345:Manganese; D005974:Glutamate-Ammonia Ligase