US EPA

6634807 

Journal Article 

Aqueous biphasic hydroformylation catalysed by protein-rhodium complexes 

Bertucci, C; Botteghi, C; Giunta, D; Marchetti, M; Paganelli, S; , 

2002 

1 

Advanced Synthesis & Catalysis
ISSN: 1615-4150
EISSN: 1615-4169 

WILEY-V C H VERLAG GMBH 

WEINHEIM 

344 

5 

556-562 

English 

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

WOS:000177246200014 

https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038583912&doi=10.1002%2f1615-4169%28200207%29344%3a5%3c556%3a%3aAID-ADSC556%3e3.0.CO%3b2-E&partnerID=40&md5=3350a526b81399261d8e2b7511e270cb
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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 degreesC and 70 atm (CO/H-2 = 1) even at very low Rh(CO)(2)(acac)/HSA catalyst concentrations. The possibility of easily recovering the Rh(l) 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. 

Aldehydes; Biphasic catalysis; Hydroformylation; Proteins; Rhodium