A semisynthetic, multicofactor artificial metalloenzyme retains independent site activity

JBIC Journal of Biological Inorganic Chemistry, Journal Year: 2025, Volume and Issue: unknown

Published: Feb. 1, 2025

Abstract Native metalloenzymes are unparalleled in their ability to perform efficient small molecule activation reactions, converting simple substrates into complex products. Most of these natural systems possess multiple metallocofactors facilitate electron transfer or cascade catalysis. While the field artificial is growing at a rapid rate, examples enzymes that leverage two distinct cofactors remain scarce. In this work, we describe new class containing different metallocofactors, incorporated through bioorthogonal strategies. Nickel-substituted rubredoxin (Ni Rd ), which structural and functional mimic [NiFe] hydrogenases, used as scaffold. Incorporation synthetic bimetallic inorganic based on macrocyclic biquinazoline ligand (M MBQ ) was accomplished using novel chelating thioether linker. Neither structure Ni active site nor M were altered upon attachment, each retained independent redox activity. Electrocatalysis observed from site, with switchability system demonstrated use catalytically inert metal centers. This –Ni platform offers avenue create multicofactor robust can be easily tuned both modifications protein scaffold moiety, applications for catalysis tandem reactivity. Graphical abstract

Language: Английский

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Enzyme sources in wastewater treatment: Their influence on enzymatic bioremediation and large-scale applications

Chemical Engineering Journal, Journal Year: 2025, Volume and Issue: unknown, P. 161891 - 161891

Published: March 1, 2025

Language: Английский

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Design of a gold nanoparticles site in an engineered lipase: an artificial metalloenzyme with enantioselective reductase-like activity

Nanoscale, Journal Year: 2024, Volume and Issue: 16(14), P. 6999 - 7010

Published: Jan. 1, 2024

The conjugation of gold complexes with proteins has proved to be interesting and effective in obtaining artificial metalloenzymes as catalysts improved properties such higher stability, activity selectivity. However, the design precise regulation their structure protein nanostructured forms level remains a challenge. Here, we have designed constructed nanoparticles-enzyme bioconjugate, by tailoring situ formation nanoparticles (AuNPs) at two specific sites on an alkalophilic lipase from Geobacillus thermocatenulatus (GTL). For this purpose, genetically modified variants GTL were created inserting unique cysteine residue into catalytic active site replacing serine (GTL-114) lid (GTL-193). enzyme, after first protein-gold coordination, induced AuNPs, generating homogeneous enzyme. size morphology AuNPs-enzyme conjugate been controlled pH conditions synthesis region where they are formed. Reductase all them was confirmed hydrogenation nitroarenes aqueous media. area seemed key for best TOF values obtained bioconjugates AuNPs site. Finally, environment asymmetric tested reduction acetophenone 1-phenylethanol medium room temperature. A high reductive conversion enantiomeric excess up 39% towards (R)-1-phenylethanol found using Au-Mt@GTL-114 10 catalyst. Moderate enantioselectivity opposite isomer also observed Au-Mt@GTL-193 conjugate.

Language: Английский

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Designing Peptide-Based Nucleophilic Catalysts Possessing Multiple Identical Active Sites for Late-Stage Chlorination of Peptides and Drugs

Organic Letters, Journal Year: 2025, Volume and Issue: unknown

Published: April 3, 2025

In the quest for developing catalysts with multiple active sites, we designed a series of methionine-based peptide prepared by classical coupling. Given widespread presence aromatic chloro-substituents and their significant pharmacokinetic properties, performance these were evaluated late-stage chlorination tyrosine residue on peptides up to octamer as well drug molecules. The operationally simple reaction conditions, excellent catalyst loading 0.25 mol %, gram-scale reactions are major highlights this method.

Language: Английский

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Engineering status of protein for improving microbial cell factories

Biotechnology Advances, Journal Year: 2023, Volume and Issue: 70, P. 108282 - 108282

Published: Nov. 7, 2023

Language: Английский

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Organic–Inorganic Porphyrinoid Frameworks for Biomolecule Sensing

ACS Sensors, Journal Year: 2023, Volume and Issue: 8(2), P. 443 - 464

Published: Jan. 23, 2023

Porphyrinoids and their analogous compounds play an important role in biosensing applications on account of unique versatile catalytic, coordination, photophysical, electrochemical properties. Their remarkable arrays properties can be finely tuned by synthetically modifying the porphyrinoid ring varying various structural parameters such as peripheral functionalization, metal covalent or physical conjugation with other organic inorganic scaffolds nanoparticles, metal–organic frameworks, polymers. organic–inorganic conjugates are not only used responsive materials but also utilized for immobilization embedding biomolecules wearable devices, fast sensing functional materials. The present review delineates impact different physicochemical specificity biosensors a range applications. newest types synthesis, modification, functionalization presented along advantages performance improvements.

Language: Английский

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The disruptive effect on the bacterial cell wall explored of the ultrasmall particle-sized Ag nanoparticles supported with Zn Cu-based hybrid nanoagents

Journal of environmental chemical engineering, Journal Year: 2024, Volume and Issue: 12(5), P. 113441 - 113441

Published: June 27, 2024

Language: Английский

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Transesterification of RNA model induced by novel dinuclear copper (II) complexes with bis-tridentate imidazole derivatives

JBIC Journal of Biological Inorganic Chemistry, Journal Year: 2023, Volume and Issue: 28(5), P. 473 - 483

Published: May 4, 2023

Language: Английский

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Structural-Based Modeling in Protein Engineering. A Must Do

The Journal of Physical Chemistry B, Journal Year: 2021, Volume and Issue: 125(24), P. 6491 - 6500

Published: June 9, 2021

Biotechnological solutions will be a key aspect in our immediate future society, where optimized enzymatic processes through enzyme engineering might an important solution for waste transformation, clean energy production, biodegradable materials, and green chemistry, example. Here we advocate the importance of structural-based bioinformatics molecular modeling tools such developments. We summarize recent experiences indicating great prediction/success ratio, suggest that early silico phase should performed studies. Moreover, demonstrate potential new technique combining Rosetta PELE, which could provide faster more automated procedure, essential broader use.

Language: Английский

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“Green” Prussian Blue Analogues as Peroxidase Mimetics for Amperometric Sensing and Biosensing

Biosensors, Journal Year: 2021, Volume and Issue: 11(6), P. 193 - 193

Published: June 10, 2021

Prussian blue analogs (PBAs) are well-known artificial enzymes with peroxidase (PO)-like activity. PBAs have a high potential for applications in scientific investigations, industry, ecology and medicine. Being stable both catalytically electrochemically active, promising the construction of biosensors biofuel cells. The “green” synthesis PO-like using oxido-reductase flavocytochrome b2 is described this study. When immobilized on graphite electrodes (GEs), obtained green-synthesized or hexacyanoferrates (gHCFs) transition noble metals produced amperometric signals response to H2O2. HCFs copper, iron, palladium other were synthesized characterized by structure, size, catalytic properties electro-mediator activities. gCuHCF, as most effective PO mimetic flower-like micro/nano superstructure, was used an H2O2-sensitive platform development glucose oxidase (GO)-based biosensor. GO/gCuHCF/GE biosensor exhibited sensitivity (710 A M−1m−2), broad linear range good selectivity when tested real samples fruit juices. We propose that gCuHCF gHCFs via may be POs oxidase-based (bio)sensors.

Language: Английский

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