There is a growing interest in implementing organometallic catalysis in the context of synthetic biology for sustainable production of chemicals. Some of the recent achievements in this field include development of bio-compatible cyclopropanation by Arnold and Balskus groups[1,2]. As a first step towards interfacing microbial metabolism we aim to utilize Artificial metalloenzymes (ArMs) to perform catalysis in the cell to augment cellular bio-synthesis. Integrating ArMs catalyzed reactions in cells also provides a springboard to apply Darwinian evolution to improve the performance of these primordial enzymes[3]. Please click Additional Files below to see the full abstract
Artificial enzymes utilizing the genetically encoded non-proteinogenic amino acid p-aminophenylalani...
Artificial metalloenzymes (ArMs) result from anchoring a metal-containing moiety within a macro mole...
The catalytic efficiency and high selectivities achieved by natural metalloenzymes are a source of i...
There is a growing interest in implementing organometallic catalysis in the context of synthetic bio...
Artificial metalloenzymes (ArMs) result from the incorportation of a catalyst precursor within a hos...
Artificial metalloenzymes (ArMs) result from the incorportation of a catalyst precursor within a hos...
Residing at the interface of chemistry and biotechnology, artificial metalloenzymes (ArMs) offer an ...
Artificial metalloenzymes (ArMs) have been proven to be a valuable concept for enantioselective cata...
Artificial metalloenzymes (ArMs) have been proven to be a valuable concept for enantioselective cata...
We report the supramolecular assembly of artificial metalloenzymes (ArMs), based on the Lactococcal ...
We report the supramolecular assembly of artificial metalloenzymes (ArMs), based on the Lactococcal ...
We report the supramolecular assembly of artificial metalloenzymes (ArMs), based on the Lactococcal ...
Artificial enzymes utilizing the genetically encoded non-proteinogenic amino acid p-aminophenylalani...
Artificial enzymes utilizing the genetically encoded non-proteinogenic amino acid p-aminophenylalani...
Artificial enzymes utilizing the genetically encoded non-proteinogenic amino acid p-aminophenylalani...
Artificial enzymes utilizing the genetically encoded non-proteinogenic amino acid p-aminophenylalani...
Artificial metalloenzymes (ArMs) result from anchoring a metal-containing moiety within a macro mole...
The catalytic efficiency and high selectivities achieved by natural metalloenzymes are a source of i...
There is a growing interest in implementing organometallic catalysis in the context of synthetic bio...
Artificial metalloenzymes (ArMs) result from the incorportation of a catalyst precursor within a hos...
Artificial metalloenzymes (ArMs) result from the incorportation of a catalyst precursor within a hos...
Residing at the interface of chemistry and biotechnology, artificial metalloenzymes (ArMs) offer an ...
Artificial metalloenzymes (ArMs) have been proven to be a valuable concept for enantioselective cata...
Artificial metalloenzymes (ArMs) have been proven to be a valuable concept for enantioselective cata...
We report the supramolecular assembly of artificial metalloenzymes (ArMs), based on the Lactococcal ...
We report the supramolecular assembly of artificial metalloenzymes (ArMs), based on the Lactococcal ...
We report the supramolecular assembly of artificial metalloenzymes (ArMs), based on the Lactococcal ...
Artificial enzymes utilizing the genetically encoded non-proteinogenic amino acid p-aminophenylalani...
Artificial enzymes utilizing the genetically encoded non-proteinogenic amino acid p-aminophenylalani...
Artificial enzymes utilizing the genetically encoded non-proteinogenic amino acid p-aminophenylalani...
Artificial enzymes utilizing the genetically encoded non-proteinogenic amino acid p-aminophenylalani...
Artificial metalloenzymes (ArMs) result from anchoring a metal-containing moiety within a macro mole...
The catalytic efficiency and high selectivities achieved by natural metalloenzymes are a source of i...