Mrutyunjay A. Nair
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View article: Biochemical Studies of a Cyanobacterial Halogenase Support the Involvement of a Dimetal Cofactor
Biochemical Studies of a Cyanobacterial Halogenase Support the Involvement of a Dimetal Cofactor Open
Halogenation is a prominent transformation in natural product biosynthesis, with over 5000 halogenated natural products known to date. Biosynthetic pathways accomplish the synthetic challenge of selective halogenation, especially at unacti…
View article: Heme Oxygenase–Like Metalloenzymes
Heme Oxygenase–Like Metalloenzymes Open
Heme oxygenase (HO)-like metalloenzymes are an emerging protein superfamily diverse in reaction outcome and mechanism. Found primarily in bacterial biosynthetic pathways, members conserve a flexible protein scaffold shared with the heme ca…
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: 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: 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 …
View article: Leveraging an enzyme/artificial substrate system to enhance cellular persulfides and mitigate neuroinflammation
Leveraging an enzyme/artificial substrate system to enhance cellular persulfides and mitigate neuroinflammation Open
A persulfide/hydrogen sulfide generation strategy through artificial substrates for 3-mercaptopyruvate sulfurtransferase (3-MST) is reported, which enhances cellular persulfides, attenuates reactive oxygen species (ROS), and alleviates inf…