Table 1.
Control reactions for the aqueous hydroformylation of 1‐octene.
| Entry | Catalyst | TON | Linear aldehyde [%] | ||||
|---|---|---|---|---|---|---|---|
| 1 | ArM: SCP‐2L A100C–1–P3–Rh[a] | 408.7 | (57.79) | 78.8 | (4.86) | ||
| 2 | Rh(acac)(CO)2 [b] | 529.7 | (53.30) | 55.3 | (0.67) | ||
| 3 | protein scaffold A100C treated with Rh[c,d] | 123.5 | (38.19) | 57.8 | (0.07) | ||
| 4 | Rh/TPPTS (1:2)[e] | 2245 | (674) | 58.9 | (0.41) | ||
| 5 | Rh/TPPTS (1:20)[e] | 700 | (190) | 56.5 | (0.08) | ||
| 6 | Rh/TPPTS (1:300)[e] | 5.4 | (3.25) | 65.9 | (8.55) | ||
| 7 | Rh/TPPTS (1:300) and SCP‐2L A100C[f] | 9.4 | (1.01) | 60.7 | (1.48) | ||
| 8 | Rh/TPPTS (1:300) and WT SCP‐2L[f] | 5.1 | (2.48) | 67.0 | (0.64) | ||
Standard conditions: 80 bar syngas (1:1), 35 °C, 625 rpm, 0.5 mL of catalyst solution and 0.5 mL of 1‐octene containing 9 % (v/v) n‐heptane and 1 % (v/v) diphenyl ether. The Rh concentration was determined by ICP‐MS for entry 1. Conversions and linear selectivities were obtained by GC analysis of a minimum of three runs. Standard deviations given in parentheses. [a] P/Rh=1.5, 23 nmol Rh. [b] 41.25 h, total volume: 0.4 mL 1‐octene, no water, 150 nmol Rh. [c] Treated with Rh and washed in the same manner as the metalloproteins. [d] 10.0 nmol Rh. [e] 30 nmol Rh. [f] Two equivalents of the protein relative to Rh.