Structural studies of staphylococcal protease. III. Binding of anions to the spin-labeled enzyme
Keyword(s):
The staphylococcal protease was coupled at the active-site serine residue with a spin-labeled analog of diisopropyl fluorophosphonate and the interaction of competitive inhibitors such as chloride and acetate anions, as well as N-carbobenzoxy-L-glutamic acid (Z-L-Glu), was investigated by electron paramagnetic resonance spectroscopy. It was observed that the addition of chloride ions to the spin-labeled enzyme increased the freedom of motion of the spin label while the presence of acetate ions and Z-L-Glu resulted in an increase in the immobilization of the spin label. These results suggest that these ions bind to the active site region in different ways.
2012 ◽
Vol 41
(3)
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pp. 156-162
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Anisotropic spin label mobilities in azurin from 95 GHz electron paramagnetic resonance spectroscopy
2003 ◽
Vol 382
(5-6)
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pp. 528-533
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2019 ◽
Vol 32
(6)
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pp. 657-660
1968 ◽
Vol 243
(10)
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pp. 2560-2568