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We hoped that additional binding sites for Rh(I), if necessary, could be found between the residues in the enzyme pocket, as for example His-159 positioned opposite Cys-25.
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28944446554
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note
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2O/acetone (δ 137.6).
-
-
-
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51
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28944454138
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note
-
In the spectrum a peak of residual oxidized papain (as its sulfinic acid) is also visible, together with a peak corresponding to the solely attached 3-hydroxy-phenacyl group resulting from the hydrolysis of the phosphite ligand. The presence of this peak seemed to be partially caused by the presence of formic acid necessary for the ESI-MS analysis.
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-
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52
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28944447095
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note
-
4 were used in the complexation step.
-
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54
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28944447622
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note
-
An additional peak appears in the ESI-MS, that could be attributed to an adduct between papain in its reduced state and one unit of Rh(I)(COD).
-
-
-
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55
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28944449434
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note
-
2 pressure was also obtained when the substrate to catalyst ratio was increased to 800 : 1.
-
-
-
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56
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28944433302
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note
-
The active site of papain is placed in a hydrophobic pocket with a cleft of about 15 Å and a groove of about 25 Å.
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