147091-70-1Relevant articles and documents
Repurposing Nonheme Iron Hydroxylases to Enable Catalytic Nitrile Installation through an Azido Group Assistance
Davidson, Madison,McNamee, Meredith,Fan, Ruixi,Guo, Yisong,Chang, Wei-Chen
, p. 3419 - 3423 (2019)
Three mononuclear nonheme iron and 2-oxoglutarate dependent enzymes, l-Ile 4-hydroxylase, l-Leu 5-hydroxylase and polyoxin dihydroxylase, are previously reported to catalyze the hydroxylation of l-isoleucine, l-leucine, and l-α-amino-δ-carbamoylhydroxyvaleric acid (ACV). In this study, we showed that these enzymes can accommodate leucine isomers and catalyze regiospecific hydroxylation. On the basis of these results, as a proof-of-concept, we demonstrated that the outcome of the reaction can be redirected by installation of an assisting group within the substrate. Specifically, instead of canonical hydroxylation, these enzymes can catalyze non-native nitrile group installation when an azido group is introduced. The reaction is likely to proceed through C - H bond activation by an Fe(IV)-oxo species, followed by azido-directed C-N bond formation. These results offer a unique opportunity to investigate and expand the reaction repertoire of Fe/2OG enzymes.
Synthesis of a key precursor for orienticin C and model study on ruthenium-mediated macrocyclization
Pearson, Anthony J.,Ciurea, Diana V.
, p. 760 - 763 (2008/09/18)
(Chemical Equation Presented) A tripeptido-arene-ruthenium complex was prepared as a key precursor for the projected synthesis of orienticin C, demonstrating that the cyclopentadienylruthenium moiety can be attached to a chloroarene in the presence of mul