Marchetti, M.

Tetrahedron Lett. 2000, 41, 3717-3720, 10.1016/S0040-4039(00)00473-1

A highly efficient and chemoselective biphasic hydroformylation of olefins was accomplished using water soluble complexes formed by the interaction between Rh(CO)2(acac) and human serum albumin (HSA), a readily available water soluble protein. A new type of shape-selectivity was observed in the hydroformylation of sterically hindered olefins.

Marchetti, M.

Adv. Synth. Catal. 2002, 344, 556, 10.1002/1615-4169(200207)344:5<556::AID-ADSC556>3.0.CO;2-E

The water‐soluble complex derived from Rh(CO)2(acac) and human serum albumin (HSA) proved to be efficient in the hydroformylation of several olefin substrates. The chemoselectivity and regioselectivity were generally higher than those obtained by using the classic catalytic systems like TPPTS‐Rh(I) (TPPTS=triphenylphosphine‐3,3′,3″‐trisulfonic acid trisodium salt). Styrene and 1‐octene, for instance, were converted in almost quantitative yields into the corresponding oxo‐aldehydes at 60 °C and 70 atm (CO/H2=1) even at very low Rh(CO)2(acac)/HSA catalyst concentrations. The possibility of easily recovering the Rh(I) compound makes the system environmentally friendly. The circular dichroism technique was useful for demonstrating the Rh(I) binding to the protein and to give information on the stability in solution of the catalytic system. Some other proteins have been used to replace HSA as complexing agent for Rh(I). The results were less impressive than those obtained using HSA and their complexes with Rh(I) were much less stable.

Jarvis, A.G.

ACS Catal. 2021, 11, 3620-3627, 10.1021/acscatal.0c05413

Protein engineering has shown widespread use in improving the industrial application of enzymes and broadening the conditions they are able to operate under by increasing their thermostability and solvent tolerance. Here, we show that protein engineering can be used to increase the thermostability of an artificial metalloenzyme. Thermostable variants of the human steroid carrier protein 2L, modified to bind a metal catalyst, were created by rational design using structural data and a 3DM database. These variants were tested to identify mutations that enhanced the stability of the protein scaffold, and a significant increase in melting temperature was observed with a number of modified metalloenzymes. The ability to withstand higher reaction temperatures resulted in an increased activity in the hydroformylation of 1-octene, with more than fivefold improvement in turnover number, whereas the selectivity for linear aldehyde remained high up to 80%.

Jarvis, A.G.; Kamer, P.C.J.

Angew. Chem. Int. Ed. 2017, 129, 13784-13788, 10.1002/ange.201705753

Kazlauskas, R.J.

ChemCatChem 2010, 2, 953-957, 10.1002/cctc.201000159

CA confidential: Replacing the active‐site zinc in carbonic anhydrase (CA) by rhodium forms a new enzymatic catalyst for cofactor‐free hydroformylation of styrene with syn gas. Unlike free rhodium, this rhodium–protein hybrid, [Rh]–CA, is regioselective (8.4:1) for linear over branched aldehyde product, which is a 40‐fold change in regioselectivity compared to free rhodium.