Aqueous olefin metathesis: recent developments and applications

• Valerio Sabatino and
• Thomas R. Ward

Beilstein J. Org. Chem. 2019, 15, 445–468, doi:10.3762/bjoc.15.39

• exploit biocompatible conditions. This review focuses on the progress made in aqueous olefin metatheses and their applications in chemical biology. Keywords: aqueous catalysis; artificial metalloenzymes; chemical biology; green chemistry; olefin metathesis; ruthenium catalysts; stapled peptides

• adamantyl group of catalyst 12. A simple filtration of the crude mixture through a cotton plug after RCM of substrate 54 yields the purified product with 53 ppm of residual ruthenium (Scheme 12). Metathesis with artificial metalloenzymes Directed evolution allows an iterative improvement by successive

• rounds of mutation and screening the performances of genetically-encoded enzymes. Hypothesizing that this tool may be applicable to the optimization of artificial metalloenzymes (ArMs) for olefin metathesis, a new-to-nature bioorthogonal reaction might be introduced in a biological system. ArMs result

Olefin metathesis catalysts embedded in β-barrel proteins: creating artificial metalloproteins for olefin metathesis

• Daniel F. Sauer,
• Johannes Schiffels,
• Takashi Hayashi,
• Ulrich Schwaneberg and
• Jun Okuda

Beilstein J. Org. Chem. 2018, 14, 2861–2871, doi:10.3762/bjoc.14.265

• /motifs exhibiting stabilities against a wide range of external influences including high salt concentrations, high temperatures and organic solvents [41][42][43][44][45]. These properties make them excellent scaffolds for the construction of artificial metalloenzymes, which is achieved by removing the

2-Methyl-2,4-pentanediol (MPD) boosts as detergent-substitute the performance of ß-barrel hybrid catalyst for phenylacetylene polymerization

• Julia Kinzel,
• Daniel F. Sauer,
• Marco Bocola,
• Marcus Arlt,
• Tayebeh Mirzaei Garakani,
• Andreas Thiel,
• Klaus Beckerle,
• Tino Polen,
• Jun Okuda and
• Ulrich Schwaneberg

Beilstein J. Org. Chem. 2017, 13, 1498–1506, doi:10.3762/bjoc.13.148

• protein FhuA; Introduction The combination of a transition metal catalyst and a protein by either dative, supramolecular or covalent means leads to so-called artificial metalloenzymes or biohybrid catalysts [1][2]. Using a non-natural catalyst, the scope of natural enzymes can be expanded or the activity

• -cell catalysts. Cells usually show increased stability towards cosolvents, pH and elevated temperatures [22][23]. A recent example in the field of artificial metalloenzymes was shown by Ward and co-workers, who used an artificial metathease in an in vivo approach. These first attempts are promising to

Artificial Diels–Alderase based on the transmembrane protein FhuA

• Hassan Osseili,
• Daniel F. Sauer,
• Klaus Beckerle,
• Marcus Arlt,
• Tomoki Himiyama,
• Tino Polen,
• Akira Onoda,
• Ulrich Schwaneberg,
• Takashi Hayashi and
• Jun Okuda

Beilstein J. Org. Chem. 2016, 12, 1314–1321, doi:10.3762/bjoc.12.124

• : artificial Diels-Alderase; biohybrid catalysis; copper enyzme; membrane protein; Introduction So-called artificial metalloenzymes have attracted attention over the last decade [1][2][3][4][5][6][7][8][9]. Incorporation of an organometallic cofactor into proteins offers new possibilities to expand the