Cited by Rational design of polymeric nanozymes with robust catalytic performance via copper-ligand coordination

In-suit generated Cu-ligand inducing full-spectrum selective photocatalytic degradation of organic pollutants containing phenol groups over Cu doping BiO2-x nanosheet: The synergistic effects of Cu-ligand and oxygen vacancies, and mechanism study DOI

Zhixiong Yang, Hui Wang, Yuan Li

et al.

Chemical Engineering Journal, Journal Year: 2024, Volume and Issue: 499, P. 155810 - 155810

Published: Sept. 16, 2024

Language: Английский

Citations

Homogeneous Oxygenase Catalysis DOI

Yujie Liang, Jialiang Wei, Xu Qiu

et al.

Chemical Reviews, Journal Year: 2018, Volume and Issue: 118(10), P. 4912 - 4945

Published: April 9, 2018

Oxygenases-catalyzed reductive activation of molecular oxygen and incorporation O atoms into an organic molecule is undoubtedly one the most attractive research areas. Typically, these oxygenation reactions proceed with high selectivity reactivity, which seldom found in its "biomimetic" chemocatalytic counterparts. Furthermore, enzymatic can avoid undesired overoxidation, frequently observed (industrial) chemical transformation. Therefore, it not surprising that tremendous attention has been paid to oxygenation. Their application synthesis steadily growing over years. The goal present Review provide a handy reference for chemists interested using homogeneous oxygenase catalysis those discovering new types biomimetic oxidations oxygenations dioxygen. In this Review, we will review recent advances reveal great achievements potentials field.

Language: Английский

Citations

151

Copper–Oxygen Dynamics in the Tyrosinase Mechanism DOI

Nobutaka Fujieda,

K. Umakoshi,

Yuta Ochi

et al.

Angewandte Chemie International Edition, Journal Year: 2020, Volume and Issue: 59(32), P. 13385 - 13390

Published: May 1, 2020

Abstract The dinuclear copper enzyme, tyrosinase, activates O 2 to form a (μ‐η :η ‐p eroxido)dicopper(II) species, which hydroxylates phenols catechols. However, the exact mechanism of phenolase reaction in catalytic site tyrosinase is still under debate. We herein report near atomic resolution X‐ray crystal structures active tyrosinases with substrate l ‐tyrosine. At their sites, CuA moved toward ‐tyrosine (CuA1 → CuA2), whose phenol oxygen directly coordinates CuA2, involving movement CuB (CuB1 CuB2). and spectroscopic analyses dioxygen‐bound demonstrated that peroxide ligand rotated, spontaneously weakening its O−O bond. Thus, migration induced by substrate‐binding accompanied rearrangement bound species so as provide one atoms access substrate's ϵ carbon atom.

Language: Английский

Citations

Homogeneous oxidative transformations mediated by copper catalyst systems DOI

Lindie Marais, Hermanus C.M. Vosloo, Andrew J. Swarts

et al.

Coordination Chemistry Reviews, Journal Year: 2021, Volume and Issue: 440, P. 213958 - 213958

Published: April 21, 2021

Language: Английский

Citations

Catalytic mechanism of the tyrosinase reaction toward the Tyr98 residue in the caddie protein DOI

Yasuyuki Matoba,

Shogo Kihara,

Naohiko Bando

et al.

PLoS Biology, Journal Year: 2018, Volume and Issue: 16(12), P. e3000077 - e3000077

Published: Dec. 31, 2018

Tyrosinase (EC 1.14.18.1), a copper-containing monooxygenase, catalyzes the conversion of phenol to corresponding ortho-quinone. The Streptomyces tyrosinase is generated as complex with “caddie” protein that facilitates transport two copper ions into active center. In our previous study, Tyr98 residue in caddie protein, which accommodated pocket center tyrosinase, has been found be converted reactive quinone through formations μ-η2:η2-peroxo-dicopper(II) and Cu(II)-dopasemiquinone intermediates. Until now—despite extensive studies for reaction based on crystallographic analysis, low-molecular-weight models, computer simulations—the catalytic mechanism unable made clear at an atomic level. To make clear, present cryo-trapped crystal structures were determined very high resolutions (1.16–1.70 Å). suggest existence important step not yet found: is, hydroxylation triggered by movement CuA, induces syn-to-anti rearrangement ligands after formation core. By rearrangement, hydroxyl group substrate placed equatorial position, allowing electrophilic attack aromatic ring Cu2O2 oxidant.

Language: Английский

Citations

Comparative effect of supercritical carbon dioxide and high pressure processing on structural changes and activity loss of oxidoreductive enzymes DOI

Krystian Marszałek, Paul Doesburg, Szymon Starzonek

et al.

Journal of CO2 Utilization, Journal Year: 2018, Volume and Issue: 29, P. 46 - 56

Published: Nov. 27, 2018

Language: Английский

Citations

Cu(ii) complexes of a tridentate N,N,O-donor Schiff base of pyridoxal: synthesis, X-ray structures, DNA-binding properties and catecholase activity DOI

Satyajit Mondal,

Moumita Chakraborty,

Antu Mondal

et al.

New Journal of Chemistry, Journal Year: 2018, Volume and Issue: 42(12), P. 9588 - 9597

Published: Jan. 1, 2018

DNA binding and catecholase activities of two Cu(ii) complexes [Cu(L₁)X] (X = N₃, NCS) pyridoxal derived ligands are reported.

Language: Английский

Citations

Metal-catalysed reactions enabled by guanidine-type ligands DOI

Xi‐Yang Cui,

Choon‐Hong Tan, Dasheng Leow

et al.

Organic & Biomolecular Chemistry, Journal Year: 2019, Volume and Issue: 17(19), P. 4689 - 4699

Published: Jan. 1, 2019

A review of metal–guanidine complexes, which are selective and powerful catalysts for organic transformations, asymmetric synthesis, polymerisation.

Language: Английский

Citations

Copper–oxygen adducts: new trends in characterization and properties towards C–H activation DOI

Jonathan De Tovar, Rébecca Leblay, Yongxing Wang

et al.

Chemical Science, Journal Year: 2024, Volume and Issue: 15(27), P. 10308 - 10349

Published: Jan. 1, 2024

Recent progresses in Cu–oxygen adducts towards recalcitrant C–H activation are reviewed with focus on Cu metalloenzymes and bioinspired synthetic models, mono- to polynuclear complexes, working under homogeneous heterogeneous catalytic conditions.

Language: Английский

Citations

Cu(II)-tyrosinase enzyme catalyst mediated synthesis of mosquito larvicidal active pyrazolidine-3,5-dione derivatives with molecular docking studies and their ichthyotoxicity analysis DOI

Velmurugan Loganathan,

Radhakrishnan Surendrakumar,

Anis Ahamed

et al.

PLoS ONE, Journal Year: 2024, Volume and Issue: 19(9), P. e0298232 - e0298232

Published: Sept. 19, 2024

The objective of this study was to develop pyrazolidine-3,5-dione derivatives with potential as environmentally friendly pesticides for pest control, specifically focusing on their efficacy larvicidal agents. A novel one-pot synthesis multicomponent ( 1a-m ) accomplished via the grindstone method using Cu(II)tyrosinase enzyme a catalyst under mild reaction conditions, yielding 84%–96%. synthesised were characterized various spectroscopic methods (mass spectrometry, elemental analysis, FT-IR, and 1 H 13 C NMR). NMR characterisation DMSO- d 6 solvent. antifeedant activities compounds screened in silico computational studies performed. activity against Culex quinquefasciatus Oreochromis mossambicus evaluated. Among compounds, compound 1c demonstrated superior (LD 50 : 9.7 μg/mL) . compared permethrin 17.1 μg/mL). Regarding activity, 1a , 1e 1f 1j 1k exhibited 100% mortality at 100 μg/mL. Molecular docking analysis performed assess binding capacity mosquito odorant-binding protein (3OGN) from results revealed that had score -10.4 kcal/mol, surpassing standard (-9.5 kcal/mol). Furthermore, DFT calculations conducted acquire theoretical data aligned experimental FT-IR results. According research, demonstrates promising larvae

Language: Английский

Citations