Mechanistic Perspective on C–N and C–S Bond Construction Catalyzed by Cytochrome P450 Enzymes DOI
Tai‐Ping Zhou,

Yakun Fan,

Jinyan Zhang

et al.

ACS Bio & Med Chem Au, Journal Year: 2024, Volume and Issue: 5(1), P. 16 - 30

Published: Nov. 27, 2024

Cytochrome P450 enzymes catalyze a large number of oxidative transformations that are responsible for natural product synthesis. Recent studies have revealed their unique ability to the formation C-N and C-S bonds, broadening biosynthetic applications. However, enzymatic mechanisms behind these reactions still unclear. This review focuses on theoretical insights into P450-catalyzed bond formation. The key roles conformational dynamics substrate radicals, influenced by enzyme environment, in modulating selectivity reactivity highlighted. Understanding reaction offers valuable guidance engineering design

Language: Английский

Structural Insights into the N–N Bond-Formation Mechanism of the Heme-Dependent Piperazate Synthase KtzT DOI

Yunyun Yang,

Yanling Li, Licheng Yao

et al.

ACS Catalysis, Journal Year: 2025, Volume and Issue: 15(2), P. 1265 - 1273

Published: Jan. 7, 2025

N–N bond formation plays a critical role in the synthesis of organic compounds and has broad applications producing dyes, pharmaceuticals, functional materials. However, is challenging due to nucleophilicity nitrogen. Here, we determined crystal structures heme-dependent enzyme, KtzT, which catalyzes cyclization l-N5-hydroxyornithine (l-N5-OH-Orn) yield l-piperazate (l-piz) by linking two intramolecular nitrogen atoms. The complex structure KtzTC197A with l-N5-OH-Orn reveals substrate-interaction network, validated through mutagenesis experiments. Notably, N5 atom substrate directly coordinates heme iron, precluding oxygen binding. This supports prior knowledge that KtzT an oxygen-independent reaction. Intriguingly, exhibits distinct conformations our crystals. Based on distance between atoms product accommodation pose KtzTC197A/l-piz structure, conformation 2 likely productive pose, while more extended 1 may be transient state facilitating entry into catalytic tunnel. A potential pathway also proposed. These findings offer structural insights for developing bio- metal-catalyzed methods formation.

Language: Английский

Citations

2
Rational Engineering of Self-Sufficient P450s to Boost Catalytic Efficiency of Carbene-Mediated C–S Bond Formation DOI

Binhao Wang,

Tai‐Ping Zhou, Yu Shen

et al.

ACS Catalysis, Journal Year: 2025, Volume and Issue: unknown, P. 5993 - 6004

Published: March 27, 2025

Language: Английский

Citations

1
Trendbericht Anorganische Chemie 2024: Nebengruppen‐ und Koordinationschemie DOI Open Access

Gabriele Hierlmeier,

Terrance J. Hadlington

Nachrichten aus der Chemie, Journal Year: 2025, Volume and Issue: 73(2), P. 56 - 64

Published: Jan. 31, 2025

Abstract Das erste heterobimetallische Dimetallocen; mit sterisch anspruchsvollen Liganden lassen sich einfach‐koordinierte Hauptgruppenverbindungen der Gruppen 13 bis 15 herstellen; neue Diazoverbindungen erlauben es, B‐R‐Einheiten und Kohlenstoffatome zu übertragen.

Citations

0
Mechanistic Perspective on C–N and C–S Bond Construction Catalyzed by Cytochrome P450 Enzymes DOI
Tai‐Ping Zhou,

Yakun Fan,

Jinyan Zhang

et al.

ACS Bio & Med Chem Au, Journal Year: 2024, Volume and Issue: 5(1), P. 16 - 30

Published: Nov. 27, 2024

Cytochrome P450 enzymes catalyze a large number of oxidative transformations that are responsible for natural product synthesis. Recent studies have revealed their unique ability to the formation C-N and C-S bonds, broadening biosynthetic applications. However, enzymatic mechanisms behind these reactions still unclear. This review focuses on theoretical insights into P450-catalyzed bond formation. The key roles conformational dynamics substrate radicals, influenced by enzyme environment, in modulating selectivity reactivity highlighted. Understanding reaction offers valuable guidance engineering design

Language: Английский

Citations

0