Monica E. Neugebauer
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View article: Synergistic Binding of the Halide and Cationic Prime Substrate of <scp>l</scp> -Lysine 4-Chlorinase, BesD, in Both Ferrous and Ferryl States
Synergistic Binding of the Halide and Cationic Prime Substrate of <span>l</span> -Lysine 4-Chlorinase, BesD, in Both Ferrous and Ferryl States Open
An aliphatic halogenase requires four substrates: 2-oxoglutarate (2OG), halide (Cl- or Br-), the halogenation target ("prime substrate"), and dioxygen. In well-studied cases, the three nongaseous substrates must bind to activate the enzyme…
View article: Phage-assisted evolution and protein engineering yield compact, efficient prime editors
Phage-assisted evolution and protein engineering yield compact, efficient prime editors Open
Prime editing enables a wide variety of precise genome edits in living cells. Here we use protein evolution and engineering to generate prime editors with reduced size and improved efficiency. Using phage-assisted evolution, we improved ed…
View article: Synergistic Binding of the Halide and Cationic Prime Substrate of the l-Lysine 4-Chlorinase, BesD, in Both Ferrous and Ferryl States
Synergistic Binding of the Halide and Cationic Prime Substrate of the l-Lysine 4-Chlorinase, BesD, in Both Ferrous and Ferryl States Open
An aliphatic halogenase requires four substrates: 2-oxoglutarate (2OG), halide (Cl − or Br − ), the halogenation target (“prime substrate”), and dioxygen. In well-studied cases, the three non-gaseous substrates must bind to activate the en…
View article: Biocatalytic control of site-selectivity and chain length-selectivity in radical amino acid halogenases
Biocatalytic control of site-selectivity and chain length-selectivity in radical amino acid halogenases Open
Biocatalytic C–H activation has the potential to merge enzymatic and synthetic strategies for bond formation. Fe II /αKG-dependent halogenases are particularly distinguished for their ability both to control selective C–H activation as wel…
View article: Evolution of an adenine base editor into a small, efficient cytosine base editor with low off-target activity
Evolution of an adenine base editor into a small, efficient cytosine base editor with low off-target activity Open
Cytosine base editors (CBEs) are larger and can suffer from higher off-target activity or lower on-target editing efficiency than current adenine base editors (ABEs). To develop a CBE that retains the small size, low off-target activity an…
View article: Regioselective control of biocatalytic C–H activation and halogenation
Regioselective control of biocatalytic C–H activation and halogenation Open
Biocatalytic C–H activation has the potential to merge enzymatic and synthetic strategies for bond formation. Fe II /αKG-dependent halogenases are particularly distinguished for their ability both to control selective C-H activation as wel…
View article: Substrate-Triggered μ-Peroxodiiron(III) Intermediate in the 4-Chloro- <scp>l</scp> -Lysine-Fragmenting Heme-Oxygenase-like Diiron Oxidase (HDO) BesC: Substrate Dissociation from, and C4 Targeting by, the Intermediate
Substrate-Triggered μ-Peroxodiiron(III) Intermediate in the 4-Chloro- <span>l</span> -Lysine-Fragmenting Heme-Oxygenase-like Diiron Oxidase (HDO) BesC: Substrate Dissociation from, and C4 Targeting by, the Intermediate Open
The enzyme BesC from the β-ethynyl-l-serine biosynthetic pathway in Streptomyces cattleya fragments 4-chloro-l-lysine (produced from l-Lysine by BesD) to ammonia, formaldehyde, and 4-chloro-l-allylglycine and can analogously fragment l-Lys…
View article: Processed files for library analysis of base editors
Processed files for library analysis of base editors Open
Analyzed data from Library Analysis of base editors. Raw FASTQs are deposited under PRJNA848090.
View article: A Substrate-triggered µ-Peroxodiiron(III) Intermediate in the 4-Chloro-L-Lysine-Fragmenting Heme-Oxygenase-like Diiron Oxidase (HDO) BesC: Substrate Dissociation from, and C4 Targeting by, the Intermediate
A Substrate-triggered µ-Peroxodiiron(III) Intermediate in the 4-Chloro-L-Lysine-Fragmenting Heme-Oxygenase-like Diiron Oxidase (HDO) BesC: Substrate Dissociation from, and C4 Targeting by, the Intermediate Open
The enzyme BesC from the β - e thynyl-L- s erine biosynthetic pathway in Streptomyces cattleya fragments 4-chloro-L-lysine (produced from L-Lysine by BesD) to ammonia, formaldehyde, and 4-chloro-L-allylglycine and can analogously fragment …