Phosphanorbornadienephosphonates as a New Type of Water-Soluble Phosphines for Biphasic Catalysis

1996 ◽  
Vol 61 (10) ◽  
pp. 3531-3533 ◽  
Author(s):  
Stéphane Lelièvre ◽  
François Mercier ◽  
François Mathey
2001 ◽  
Vol 79 (5-6) ◽  
pp. 1040-1048 ◽  
Author(s):  
H Gulyás ◽  
A Dobó ◽  
J Bakos

Cyclic and bicyclic sulfates have been prepared from commonly available alcohols. Nucleophilic cleavage of the cyclic sulfates affords a new type of water-soluble mono- and ditertiary phophines bearing -OSO3Li groups in distinguished positions in the molecular framework. Both phosphines have amphiphilic character. Reactions of the chiral 2 and the dppp analogue 5 with [Rh(COD)Cl]2 and Pt(PhCN)2Cl2 provide novel zwitterionic complexes. Rhodium complexes of 2 and 5 have been successfully applied in liquid biphasic hydroformylation of styrene and octene-1. When the rhodium complex of 5 was used as catalyst in hydroformylation of styrene, less then 4 ppm rhodium could be detected in the organic phase.Key words: cyclic sulfates, water soluble phosphines, amphiphilic character, Rh complexes, Pt complexes, hydroformylation.


1993 ◽  
Vol 462 (1-2) ◽  
pp. 103-106 ◽  
Author(s):  
François Mercier ◽  
François Mathey

ChemInform ◽  
2010 ◽  
Vol 23 (49) ◽  
pp. no-no
Author(s):  
T. N. MITCHELL ◽  
K. HEESCHE-WAGNER

ChemInform ◽  
2010 ◽  
Vol 31 (9) ◽  
pp. no-no
Author(s):  
Kattesh V. Katti ◽  
Douglas E. Berning ◽  
Charles J. Smith ◽  
Hariprasad Gali

2020 ◽  
Vol 367 (20) ◽  
Author(s):  
Yulia V Bertsova ◽  
Ilya P Oleynikov ◽  
Alexander V Bogachev

ABSTRACT The cytoplasmic fumarate reductase of Klebsiella pneumoniae (FRD) is a monomeric protein which contains three prosthetic groups: noncovalently bound FMN and FAD plus a covalently bound FMN. In the present work, NADH is revealed to be an inherent electron donor for this enzyme. We found that the fumarate reductase activity of FRD significantly exceeds its NADH dehydrogenase activity. During the catalysis of NADH:fumarate oxidoreductase reaction, FRD turnover is limited by a very low rate (∼10/s) of electron transfer between the noncovalently and covalently bound FMN moieties. Induction of FRD synthesis in K. pneumoniae cells was observed only under anaerobic conditions in the presence of fumarate or malate. Enzymes with the FRD-like domain architecture are widely distributed among various bacteria and apparently comprise a new type of water-soluble NADH:fumarate oxidoreductases.


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