Direct Z-Scheme Polymer/Polymer Double-Shell Hollow Nanostructures for Efficient NADH Regeneration and Biocatalytic Artificial Photosynthesis under Visible Light DOI
Song Wang,

Xiewen Wu,

Jing Fang

et al.

ACS Catalysis, Journal Year: 2023, Volume and Issue: 13(7), P. 4433 - 4443

Published: March 17, 2023

The design of a highly efficient polymer photocatalyst is an essential prerequisite for photo-biocatalysis in polymer–enzyme coupled system, which offers important platform the synthesis pharmaceuticals and fine chemicals. However, current polymers still suffer drawbacks poor water wettability, low visible light absorption, high recombination rate photoinduced electron/hole pairs, severely limit their application photo-biocatalysis. Herein, we demonstrate polymer/polymer double-shell hollow nanostructure (PCN@PDBTS-HN) via facile two-step polymerization with polymeric carbon nitride (PCN) poly-dibenzothiophene sulfone (PDBTS) as internal external shells, respectively. covalent connection those two layers ensures spontaneous electron transfer from PDBTS to PCN, reflected X-ray photoelectron spectroscopy (XPS), paramagnetic resonance (EPR), fluorescence spectra, could effectively accelerate charge separation migration. Thanks its improved light-harvesting, increased hydrophilicity, enhanced redox capacity, obtained PCN@PDBTS-HN demonstrates excellent catalytic efficiency visible-light-promoted NADH regeneration conversion 85.4% being achieved 40 min (turnover frequency 0.859 mmol g–1 h–1). This value 1.4 2.6 times higher than that pristine PCN PDBTS, respectively, indicating role Z-scheme heterojunction improving efficiency. In addition, also displays photocatalytic selectivity 1,4-NADH regeneration, remarkable photostability, good biocompatibility. A total amount 2.12 mM methanol 8.39 l-glutamate was accumulated polymer/alcohol dehydrogenase (YADH) polymer/glutamate (GDH) implying flexibility chemical production photo-biocatalytic approach.

Language: Английский

Iron Heme Enzyme-Catalyzed Cyclopropanations with Diazirines as Carbene Precursors: Computational Explorations of Diazirine Activation and Cyclopropanation Mechanism DOI
Torben Rogge, Qingyang Zhou, Nicholas J. Porter

et al.

Journal of the American Chemical Society, Journal Year: 2024, Volume and Issue: 146(5), P. 2959 - 2966

Published: Jan. 25, 2024

The mechanism of cyclopropanations with diazirines as air-stable and user-friendly alternatives to commonly employed diazo compounds within iron heme enzyme-catalyzed carbene transfer reactions has been studied by means density functional theory (DFT) calculations model systems, quantum mechanics/molecular mechanics (QM/MM) calculations, molecular dynamics (MD) simulations the cyclopropanation transition state in enzyme active site. reaction is initiated a direct diazirine-diazo isomerization occurring site enzyme. In contrast, an proceeding via formation free intermediate lieu direct, one-step process was observed for systems. Subsequent benzyl acrylate takes place through stepwise C–C bond diradical intermediate, delivering cyclopropane product. origin diastereo- enantioselectivity investigated MD simulations, which indicate preferred cis-cyclopropane steric control.

Language: Английский

Citations

14
Enzyme engineering for biocatalysis DOI Creative Commons
Caroline E. Paul, Ulf Hanefeld, Frank Hollmann

et al.

Molecular Catalysis, Journal Year: 2024, Volume and Issue: 555, P. 113874 - 113874

Published: Jan. 31, 2024

Contemporary Biocatalysis heavily relies on enzyme engineering as natural enzymes frequently lack the requisite attributes for effective organic synthesis. The inherent limitations in stability, catalytic activity, and selectivity of wild-type often hinder their suitability chemical Over past 25 years, there has been an unprecedented advancement protein tools, empowering enzymologists to customise precisely meet demands In this discussion, we delineate some most crucial techniques significance facilitating

Language: Английский

Citations

11
Precision Engineering of the Co‐immobilization of Enzymes for Cascade Biocatalysis DOI

Zhiyuan Luo,

Li Qiao, Haomin Chen

et al.

Angewandte Chemie International Edition, Journal Year: 2024, Volume and Issue: 63(22)

Published: April 1, 2024

Abstract The design and orderly layered co‐immobilization of multiple enzymes on resin particles remain challenging. In this study, the SpyTag/SpyCatcher binding pair was fused to N‐terminus an alcohol dehydrogenase (ADH) aldo‐keto reductase (AKR), respectively. A non‐canonical amino acid (ncAA), p ‐azido‐L‐phenylalanine (p‐AzF), as anchor for covalent bonding enzymes, genetically inserted into preselected sites in AKR ADH. Employing two bioorthogonal counterparts azide–alkyne cycloaddition immobilization ADH enabled sequential dual‐enzyme coating porous microspheres. ordered reactor subsequently used synthesize ( S )‐1‐(2‐chlorophenyl)ethanol asymmetrically from corresponding prochiral ketone, enabling situ regeneration NADPH. exhibited a high catalytic conversion 74 % good reproducibility, retaining 80 its initial activity after six cycles. product had 99.9 ee, which that maintained each cycle. Additionally, double‐layer method significantly increased enzyme loading capacity, approximately 1.7 times greater than traditional single‐layer immobilization. More importantly, it simultaneously both purification carriers, thus providing convenient approach facilitate cascade biocatalysis.

Language: Английский

Citations

9
Extensive gene mining and facile engineering of a novel carbonyl reductase for asymmetric synthesis of anti-aging (S)-Pro-Xylane from d-xylose DOI
Zhe Dou,

Penghui Hu,

Linlin Song

et al.

International Journal of Biological Macromolecules, Journal Year: 2025, Volume and Issue: unknown, P. 140976 - 140976

Published: Feb. 1, 2025

Language: Английский

Citations

1
Unraveling the molecular basis of substrate specificity and halogen activation in vanadium-dependent haloperoxidases DOI Creative Commons

Pierre Zeides,

Kathrin Bellmann‐Sickert, Ru Zhang

et al.

Nature Communications, Journal Year: 2025, Volume and Issue: 16(1)

Published: Feb. 28, 2025

Abstract Vanadium-dependent haloperoxidases (VHPOs) are biotechnologically valuable and operationally versatile biocatalysts. VHPOs share remarkable active-site structural similarities yet display variable reactivity selectivity. The factors dictating substrate specificity and, thus, a general understanding of VHPO reaction control still need to be discovered. This work’s strategic single-point mutation in the cyanobacterial bromoperoxidase Am facilitates selectivity switch allow aryl chlorination. induces loop formation that interacts with neighboring protein monomer, creating tunnel active sites. Structural analysis substrate-R425S-mutant complex reveals substrate-binding site at interface two adjacent units. There, residues Glu139 Phe401 interact arenes, extending residence time close vanadate cofactor stabilizing intermediates. Our findings validate long-debated existence direct binding provide detailed mechanistic understanding. work will pave way for broader application diverse chemical processes.

Language: Английский

Citations

1
Rational engineering of a thermostable α-oxoamine synthase biocatalyst expands the substrate scope and synthetic applicability DOI Creative Commons
Ben Ashley, Sam Mathew,

Mariyah Sajjad

et al.

Communications Chemistry, Journal Year: 2025, Volume and Issue: 8(1)

Published: March 13, 2025

Abstract Carbon-carbon bond formation is one of the key pillars organic synthesis. Green, selective and efficient biocatalytic methods for such are therefore highly desirable. The α-oxoamine synthases (AOSs) a class pyridoxal 5’-phosphate (PLP)-dependent, irreversible, carbon-carbon bond-forming enzymes, which have been limited previously by their narrow substrate specificity requirement acyl-CoA thioester substrates. We recently characterized thermophilic enzyme from Thermus thermophilus ( Th AOS) with much broader scope described its use in chemo-biocatalytic cascade process to generate pyrroles good yields timescales. Herein, we report structure-guided engineering AOS arrive at variants able greatly expanded range amino acid simplified N-acetylcysteamine (SNAc) acyl-thioester crystal structure improved V79A variant bound PLP: l -penicillamine external aldimine ligand, provides insight into properties engineered biocatalyst.

Language: Английский

Citations

1
Biomass-derived nanocellulose aerogel enable highly efficient immobilization of laccase for the degradation of organic pollutants DOI

Dingsheng Wu,

Pengfei Lv, Quan Feng

et al.

Bioresource Technology, Journal Year: 2022, Volume and Issue: 356, P. 127311 - 127311

Published: May 12, 2022

Language: Английский

Citations

33
Enhanced Photocatalytic Efficiency in Visible-Light-Induced NADH Regeneration by Intramolecular Electron Transfer DOI

Xiewen Wu,

Song Wang,

Jing Fang

et al.

ACS Applied Materials & Interfaces, Journal Year: 2022, Volume and Issue: 14(34), P. 38895 - 38904

Published: Aug. 20, 2022

Inspired by natural photosynthesis, photocatalytic NADH regeneration has drawn increasing interest in the recent decade as it provides a perfect approach for NAD+ reduction into NADH, which can be further consumed oxidordeuctase enzymatic redox reactions. However, two issues still remain unsolved this procedure. First, efficiency hydrogenation requires improvement. Second, rhodium electron mediator [Cp*Rh(bpy)H2O]2+ (M), is always required selective 1,4-NADH regeneration, difficult to recover because of its good solubility aqueous solution. Given high price M, highly wasteful and inefficient if only spends once. Here, we report Cp*Rh(bpy)Cl implanted conjugated microporous polymer DTS/Rh@CMPs employed effective visible light photocatalysts situ without using additional M. In addition, insertion Rh complex skeleton, demonstrated UV-vis, fluorescence, photocurrent electrochemical impedance, dramatically improves absorption capacity separation transfer efficiency. Compared with that DTS@CMP-1 an enhanced reaction yield 33% was determined DTS/Rh@CMP-1 suggesting intramolecular better activity than intermolecular reduction. Moreover, rooted firmly framework, negligible loss conversion decrease are observed. When coupled yeast alcohol dehydrogenase (YADH, from Saccharomyces cerevisiae), 1.36 mM methanol accumulated, implying excellent biocompatibility feasibility photobiocatalysis formaldehyde hydrogenation.

Language: Английский

Citations

32
Molecular Catalysis for the Chemistry of the future: a perspective DOI
Jeong Woo Han, Frank Hollmann, Rafael Luque

et al.

Molecular Catalysis, Journal Year: 2022, Volume and Issue: 522, P. 112233 - 112233

Published: March 25, 2022

Language: Английский

Citations

29
Cascades of Evolved Enzymes for the Synthesis of Complex Molecules DOI Creative Commons
Katrin Rosenthal, Uwe T. Bornscheuer, Stephan Lütz

et al.

Angewandte Chemie International Edition, Journal Year: 2022, Volume and Issue: 61(39)

Published: Aug. 26, 2022

Abstract Thanks to advances in enzyme discovery and protein engineering combined with the development of enzymatic multistep reaction cascades, new efficient routes for drug synthesis have been created that are superior chemical syntheses. This supports goal pharmaceutical industries move more sustainable environmentally friendly processes. Recently described outstanding examples include biocatalytic cascade syntheses cyclic dinucleotide MK‐1454, molnupiravir, islatravir, as well fixation CO 2 make starch using an artificial cascade.

Language: Английский

Citations

29