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. 2005 Mar 16;102(13):4683–4687. doi: 10.1073/pnas.0409684102

Table 3. Selected results for the optimization of the performance of [η6-(arene)Ru(Biot-p-L)Cl]⊂(strept)avidin as an artificial metalloenzyme for the transfer hydrogenation of acetophenone derivatives 2a-c by using formate·boric acid as a reducing agent in 0.15 M Mops buffer.

Entry Ligand η6-arene Protein Substrate Temperature, °C Time, h Conversion, % ee, %
1 Biot-p-L p-cymene Sav 2a 45 40 40 66 (R)
2 Biot-p-L Benzene Sav 2a 45 40 30 63 (S)
3 Biot-p-L p-cymene Sav 2a 55 64 82 68 (R)
4 Biot-p-L p-cymene P64G Sav 2a 55 64 90 85 (R)
5 Biot-p-L p-cymene P64G Sav 2b 55 64 97 89 (R)
6 Biot-p-L p-cymene P64G Sav 2c 55 64 92 94 (R)
7 Biot-p-L p-cymene P64G S112 G Sav 2a 55 40 Quantitative 67 (R)
8 Biot-p-L p-cymene P64G S112 G Sav 2b 55 40 Quantitative 88 (R)
9 Biot-p-L p-cymene P64G S112 G Sav 2c 55 40 Quantitative 90 (R)
10 Biot-p-L Benzene P64G Sav 2c 45 64 34 57 (S)
11 Biot-p-L Benzene P64G Sav 2c 55 64 44 44 (S)

All catalytic runs were carried out at pHinitial = 6.25 by using the mixed buffer HCO2Na (0.5 M) + B(OH)3 (0.47 M) combined with Mops (0.15 M) with a Ru/substrate 2 a-c/formate ratio of 1:100:4,500. Conversions and enantioselectivity were determined by HPLC on Chiralcel OB-H.