The Experts below are selected from a list of 3 Experts worldwide ranked by ideXlab platform
Scott J Miller - One of the best experts on this subject based on the ideXlab platform.
-
functional analysis of an aspartate based Epoxidation catalyst with amide to alkene peptidomimetic catalyst analogues
Angewandte Chemie, 2008Co-Authors: Charles E Jakobsche, Gorka Peris, Scott J MillerAbstract:The biosynthesis of natural products that contain epoxides represents a powerful stimulus for the study of “epoxidase” enzymes.[i] Likewise, these processes have inspired a generation of science focused on small molecule catalysts that mediate selective Epoxidations through a variety of mechanisms.[ii] With respect to the naturally occurring epoxidases, the mechanistic basis of O-atom transfer is often associated with the chemistry of either flavinoid cofactors, P450 enzymes containing a heme group, or chloroperoxidases that lead to stepwise ring formation.[iii] In thinking about the known biosynthetic apparatus for epoxide formation, we became curious about an alternative mode for O-atom transfer – one based on functional groups available in proteins, but perhaps not well-documented in the biosynthesis of epoxides. In particular, we speculated and recently showed that aspartic-acid-containing peptides (e.g., 1; Figure 1a) might shuttle between the side-chain carboxylic acid and the corresponding peracid (e.g., 2) creating a catalytic cycle competent for asymmetric Epoxidation with turnover of the aspartate-derived catalyst. Such an approach is orthogonal to the Julia-Colonna Epoxidation, a complementary peptide-based Epoxidation based on a nucleophilic mechanism.[iv] Indeed, as shown in Figure 1b, this new electrophilic Epoxidation catalytic cycle mediates the asymmetric Epoxidation of substrates like 3 to give products like 4 with up to 92% ee.[v]
Charles E Jakobsche - One of the best experts on this subject based on the ideXlab platform.
-
functional analysis of an aspartate based Epoxidation catalyst with amide to alkene peptidomimetic catalyst analogues
Angewandte Chemie, 2008Co-Authors: Charles E Jakobsche, Gorka Peris, Scott J MillerAbstract:The biosynthesis of natural products that contain epoxides represents a powerful stimulus for the study of “epoxidase” enzymes.[i] Likewise, these processes have inspired a generation of science focused on small molecule catalysts that mediate selective Epoxidations through a variety of mechanisms.[ii] With respect to the naturally occurring epoxidases, the mechanistic basis of O-atom transfer is often associated with the chemistry of either flavinoid cofactors, P450 enzymes containing a heme group, or chloroperoxidases that lead to stepwise ring formation.[iii] In thinking about the known biosynthetic apparatus for epoxide formation, we became curious about an alternative mode for O-atom transfer – one based on functional groups available in proteins, but perhaps not well-documented in the biosynthesis of epoxides. In particular, we speculated and recently showed that aspartic-acid-containing peptides (e.g., 1; Figure 1a) might shuttle between the side-chain carboxylic acid and the corresponding peracid (e.g., 2) creating a catalytic cycle competent for asymmetric Epoxidation with turnover of the aspartate-derived catalyst. Such an approach is orthogonal to the Julia-Colonna Epoxidation, a complementary peptide-based Epoxidation based on a nucleophilic mechanism.[iv] Indeed, as shown in Figure 1b, this new electrophilic Epoxidation catalytic cycle mediates the asymmetric Epoxidation of substrates like 3 to give products like 4 with up to 92% ee.[v]
Gorka Peris - One of the best experts on this subject based on the ideXlab platform.
-
functional analysis of an aspartate based Epoxidation catalyst with amide to alkene peptidomimetic catalyst analogues
Angewandte Chemie, 2008Co-Authors: Charles E Jakobsche, Gorka Peris, Scott J MillerAbstract:The biosynthesis of natural products that contain epoxides represents a powerful stimulus for the study of “epoxidase” enzymes.[i] Likewise, these processes have inspired a generation of science focused on small molecule catalysts that mediate selective Epoxidations through a variety of mechanisms.[ii] With respect to the naturally occurring epoxidases, the mechanistic basis of O-atom transfer is often associated with the chemistry of either flavinoid cofactors, P450 enzymes containing a heme group, or chloroperoxidases that lead to stepwise ring formation.[iii] In thinking about the known biosynthetic apparatus for epoxide formation, we became curious about an alternative mode for O-atom transfer – one based on functional groups available in proteins, but perhaps not well-documented in the biosynthesis of epoxides. In particular, we speculated and recently showed that aspartic-acid-containing peptides (e.g., 1; Figure 1a) might shuttle between the side-chain carboxylic acid and the corresponding peracid (e.g., 2) creating a catalytic cycle competent for asymmetric Epoxidation with turnover of the aspartate-derived catalyst. Such an approach is orthogonal to the Julia-Colonna Epoxidation, a complementary peptide-based Epoxidation based on a nucleophilic mechanism.[iv] Indeed, as shown in Figure 1b, this new electrophilic Epoxidation catalytic cycle mediates the asymmetric Epoxidation of substrates like 3 to give products like 4 with up to 92% ee.[v]
