137641-43-1Relevant academic research and scientific papers
Cross metathesis of methyl oleate (MO) with terminal, internal olefins by ruthenium catalysts: Factors affecting the efficient MO conversion and the selectivity
Awang, Nor Wahida,Tsutsumi, Ken,Hu?táková, Barbora,Yusoff, Siti Fairus M.,Nomura, Kotohiro,Yamin, Bohari M.
, p. 100925 - 100930 (2016/11/09)
Cross metathesis (CM) reactions of methyl oleate (MO) with cis-4-octene (OC), cis-stilbene (CS) using RuCl2(PCy3)(IMesH2)(CHPh) [IMesH2 = 1,3-bis(2,4,6-trimethylphenyl)imidazolin-2-ylidene; Cy = cyclohexyl] afforded CM products with high MO conversion and high selectivity under high molar (OC/MO, CS/MO) ratios; CM with cis-1,4-diacetoxy-2-butene also afforded metathesis products with high MO conversion under certain conditions. The efficient CM with allyltrimethylsilane proceeded with high activity, whereas the CM with glycidyl ether, β-pinene, and vanillylidenacetone proceeded with low MO conversion.
Enzyme-substrate complementarity governs access to a cationic reaction manifold in the P450BM3-catalysed oxidation of cyclopropyl fatty acids
Cryle, Max J.,Hayes, Patricia Y.,De Voss, James J.
, p. 15994 - 15999 (2013/02/21)
The products of cytochrome P450BM3-catalysed oxidation of cyclopropyl-containing dodecanoic acids are consistent with the presence of a cationic reaction intermediate, which results in efficient dehydrogenation of the rearranged probes by the enzyme. These results highlight the importance of enzyme-substrate complementarity, with a cationic intermediate occurring only when the probes used begin to diverge from ideal substrates for this enzyme. This also aids in reconciling literature reports supporting the presence of cationic intermediates with certain cytochrome P450 enzyme/substrate pairs.
