Phosphorus–oxygen bond formation on organo-capped tricobalt centres via phosphorus–hydrogen or phosphorus–phosphorus bond scission

Author(s):  
Gillian A. Acum ◽  
Martin J. Mays ◽  
Paul R. Raithby ◽  
Harold R. Powell ◽  
Gregory A. Solan
Author(s):  
Ayesha Jalil ◽  
Yaxin O Yang ◽  
Zhendong Chen ◽  
Rongxuan Jia ◽  
Tianhao Bi ◽  
...  

: Hypervalent iodine reagents are a class of non-metallic oxidants have been widely used in the construction of several sorts of bond formations. This surging interest in hypervalent iodine reagents is essentially due to their very useful oxidizing properties, combined with their benign environmental character and commercial availability from the past few decades ago. Furthermore, these hypervalent iodine reagents have been used in the construction of many significant building blocks and privileged scaffolds of bioactive natural products. The purpose of writing this review article is to explore all the transformations in which carbon-oxygen bond formation occurred by using hypervalent iodine reagents under metal-free conditions


ChemInform ◽  
2008 ◽  
Vol 39 (1) ◽  
Author(s):  
Laetitia Coudray ◽  
Isabelle Abrunhosa-Thomas ◽  
Jean-Luc Montchamp

1970 ◽  
Vol 3 (2) ◽  
pp. 241-242 ◽  
Author(s):  
T. H. Kinstle ◽  
W. R. Oliver ◽  
L. A. Ochrymowycz

ChemInform ◽  
2010 ◽  
Vol 41 (20) ◽  
Author(s):  
Sophie Romain ◽  
Laura Vigara ◽  
Antoni Llobet

1977 ◽  
Vol 165 (3) ◽  
pp. 575-580 ◽  
Author(s):  
B Bartholomew ◽  
K S Dodgson ◽  
G W J Matcham ◽  
D J Shaw ◽  
G F White

The hydrolysis was studied of potassium (+)-octan-2-yl sulphate by two analogous, optically stereospecific, secondary alkylsulphohydrolases purified from two detergent-degrading micro-organisms, Comamonas terrigena and Pseudomonas C12B. Polarimetry studies have shown that (+)-octan-2-yl sulphate prepared from (+)-octan-2-ol is hydrolysed by both enzymes to yield (-)-octan-2-ol. This inversion of configuration implies that the enzymes are catalysing the scission of the C-O bond of the C-O-S linkage, a type of bond scission apparently not hitherto encountered among hydrolytic enzymes acting on ester bonds. Enzymic hydrolysis of potassium (+)-octan-2-yl sulphate in the presence of H218O and analysis of hydrolysis products for the presence of 18O has confirmed that C-O bond scission (and not O-S bond scission) occurs with both enzymes.


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