Jiakun Xu

ORCID: 0000-0002-8069-9717
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About
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Research Areas
  • X-ray Diffraction in Crystallography
  • Crystallization and Solubility Studies
  • Hemoglobin structure and function
  • Metal-Organic Frameworks: Synthesis and Applications
  • Magnetism in coordination complexes
  • Crystal structures of chemical compounds
  • Porphyrin Metabolism and Disorders
  • Electrochemical sensors and biosensors
  • Pharmacogenetics and Drug Metabolism
  • Enzyme-mediated dye degradation
  • Crystallography and molecular interactions
  • Metal complexes synthesis and properties
  • Heme Oxygenase-1 and Carbon Monoxide
  • Covalent Organic Framework Applications
  • Advanced biosensing and bioanalysis techniques
  • Asymmetric Hydrogenation and Catalysis
  • Nanoparticle-Based Drug Delivery
  • Synthesis and biological activity
  • Electrospun Nanofibers in Biomedical Applications
  • Synthesis and Characterization of Heterocyclic Compounds
  • Enzyme Catalysis and Immobilization
  • Photosynthetic Processes and Mechanisms
  • Carbon dioxide utilization in catalysis
  • Alkaloids: synthesis and pharmacology
  • Pharmaceutical and Antibiotic Environmental Impacts

Chinese Academy of Fishery Sciences
2014-2025

Ministry of Agriculture and Rural Affairs
2019-2024

National Marine Life Center
2020-2021

Qingdao National Laboratory for Marine Science and Technology
2019-2020

Qingdao Center of Resource Chemistry and New Materials
2018-2020

Ministère de l'Agriculture et de la Souveraineté alimentaire
2020

Harbin Medical University
2019

Ocean University of China
2008-2015

Ministry of Education of the People's Republic of China
2014

Qingdao Institute of Bioenergy and Bioprocess Technology
2014

Cu2O/CuO nanosheets in-situ grown on Cu-Carbon cloths (Cu-CCs), namely Cu2O/CuO@Cu-CCs, are constructed by a simple strategy with electroless copper plating, chemical etching, and thermal dehydration. The as-prepared material is directly used as binder-free electrodes for supercapacitors (SCs). CCs coated Cu, the current collector, can effectively promote charge collection electron transfer, while hierarchical provide massive active sites fast faradic reactions. composite electrode exhibits...

10.3389/fchem.2019.00420 article EN cc-by Frontiers in Chemistry 2019-06-06

Highly regioselective <italic>O</italic>-demethylation of aromatic ethers related to the bioconversion lignin was achieved by H<sub>2</sub>O<sub>2</sub>-dependent engineered P450BM3 enzymes with assistance a dual-functional small molecule (DFSM) for first time.

10.1039/d0cy00241k article EN Catalysis Science & Technology 2020-01-01

Cytochrome P450 enzymes (P450s) catalyze the monooxygenation of various organic substrates. These are fascinating and promising biocatalysts for synthetic applications. Despite impressive abilities P450s in oxidation C-H bonds, their practical applications restricted by intrinsic drawbacks, such as poor stability, low turnover rates, need expensive cofactors (e.g., NAD(P)H), narrow scope useful non-native issues may be overcome through general strategy protein engineering, which focuses on...

10.1002/chem.201806383 article EN Chemistry - A European Journal 2019-01-30

Approaches to degradation of industrial dyes are desirable, which bioremediation is more favorable. In addition the use native enzymes, rational design artificial enzymes provides an alternative approach. Meanwhile, few designs can achieve a catalytic activity comparable that enzymes. We have previously designed two generations dye-decolorizing peroxidases (DyPs) in myoglobin (Mb) by introduction Tyr43 and Trp138 heme pocket; however, moderate. To improve DyP, we herein third generation...

10.1021/acscatal.9b02226 article EN ACS Catalysis 2019-07-29

Protein design has received much attention in the last decades. With an additional disulfide bond to enhance protein stability, human A15C neuroglobin (Ngb) is ideal scaffold for heme enzyme design. In this study, we rationally converted Ngb into a multifunctional peroxidase by replacing axial His64 with Asp residue, where Asp64 and native Lys67 at distal site were proposed act as acid–base catalytic couple H2O2 activation. Kinetic studies showed that efficiency of A15C/H64D was higher...

10.1021/acs.inorgchem.0c03777 article EN Inorganic Chemistry 2021-02-04

Functional enzyme design has made tremendous progress, but designer enzymes with activities comparable to those of natural are still limited. In this study, we rationally engineered a functional peroxidase catalytic binding site guaiacol in model protein, myoglobin (Mb), by replacing Phe46 serine (F46S mutation), together distal Tyr the heme pocket (F43Y mutation). The double mutant F43Y/F46S Mb exhibited an overall efficiency that exceeds most peroxidases and is similar efficient...

10.1021/acscatal.9b05080 article EN ACS Catalysis 2019-12-19

The treatment of environmental pollutants such as synthetic dyes and lignin has received much attention, especially for biotechnological treatments using both native artificial metalloenzymes. In this study, we designed engineered an efficient peroxidase the O2 carrier myoglobin (Mb) a protein scaffold by four mutations (F43Y/T67R/P88W/F138W), which combines key structural features natural peroxidases presence conserved His-Arg pair Tyr/Trp residues close to heme active center. Kinetic...

10.3390/ijms23010413 article EN International Journal of Molecular Sciences 2021-12-30

Tetracyclines are one class of widely used antibiotics. Meanwhile, due to abuse and improper disposal, they often detected in wastewater, which causes a series environmental problems poses threat human health safety. As an efficient environmentally friendly method, enzymatic catalysis has attracted much attention. In previous studies, we have designed peroxidase (F43Y/P88W/F138W Mb, termed YWW Mb) based on the protein scaffold myoglobin (Mb), O2 carrier, by modifying heme active center...

10.3390/molecules27248660 article EN cc-by Molecules 2022-12-07

With the demand nowadays for blue dyes, it is of practical importance to develop a green and efficient biocatalyst production indigo. The design artificial enzymes has been shown be attractive in recent years. In previous study, we engineered single mutant sperm whale myoglobin, F43Y Mb, with novel Tyr-heme cross-link. this found that can efficiently catalyze oxidation indole indigo, yield as high 54% compared highest (∼20%) reported date literature. By further modifying heme active site,...

10.1039/c8ra07825d article EN cc-by-nc RSC Advances 2018-01-01

Chitin deacetylase (CDA) can catalyze the deacetylation of chitin to produce chitosan. In this study, we identified and characterized a gene from Euphausia superba (EsCDA-9k), soluble recombinant protein molecular weight 45 kDa was cloned, expressed, purified. The full-length cDNA sequence EsCDA-9k 1068 bp long encoded 355 amino acid residues that contained typical domain structure carbohydrate esterase family 4. predicted three-dimensional showed 67.32% homology with Penaeus monodon....

10.3390/ijms25042075 article EN International Journal of Molecular Sciences 2024-02-08

Hydrogen peroxide-dependent oxidation of indole producing indigo has been catalyzed by engineered myoglobins (Mbs). We have investigated a series H64D mutants Mbs in which Asp-64 accelerates the reaction with hydrogen peroxide and stabilizes resulting active species: compound I (iron oxo-ferryl porphyrin π-cation radical). The catalytic activity depends on amino acids at 68 107 positions H64D/V68I/I107A mutant gave highest activity, suggesting that side chains Ile-68 Ala-107 provide...

10.1039/c2cy00427e article EN Catalysis Science & Technology 2011-12-13

With the increasing demand for blue dyes, it is of vital importance to develop a green and efficient biocatalyst produce indigo. This study constructed hydrogen peroxide-dependent catalytic system direct conversion indole indigo using P450BM3 with assistance dual-functional small molecules (DFSM). The arrangements amino acids at 78, 87, 268 positions influenced activity. F87G/T268V mutant gave highest activity kcat 1402 min-1 yield 73%. F87A/T268V was found product chemoselectivity as high...

10.3390/ijms24032395 article EN International Journal of Molecular Sciences 2023-01-25

Synthetic dyes such as malachite green (MG) have a wide range of applications. Meanwhile, they bring great challenges for environmental security and cause potential damages to human health. Compared with traditional approaches, enzymatic catalysis is an emerging technique wastewater treatment. As alternatives natural enzymes, artificial enzymes received much attention In previous studies, we rationally designed based on myoglobin (Mb), by introducing distal histidine (F43H mutation) creating...

10.1039/d1ra02202d article EN cc-by-nc RSC Advances 2021-01-01

The design of functional metalloenzymes is attractive for the biosynthesis biologically important compounds, such as phenoxazinones and phenazines catalyzed by native phenoxazinone synthase (PHS). To heme enzymes, we used myoglobin (Mb) a model protein introduced an artificial CXXC motif into distal pocket F46C L49C mutations, which forms de novo disulfide bond, confirmed X-ray crystal structure. We further catalytic Tyr43 found that F43Y/F46C/L49C Mb triple mutant previously designed...

10.1021/acs.biochem.1c00554 article EN Biochemistry 2021-10-19

It is desired to design and construct more efficient enzymes with better performance catalyze carbene N-H insertions for the synthesis of bioactive molecules. To this end, we exploited designed a series human neuroglobin (Ngb) mutants. As shown in study, double mutant, A15C/H64G Ngb, an additional disulfide bond modified heme active site, exhibited yields up >99% total turnover numbers 33000 catalyzing aromatic amine derivatives, including those large size such as 1-aminopyrene. Moreover,...

10.1021/acs.inorgchem.3c02855 article EN Inorganic Chemistry 2023-09-29
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