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@ARTICLE{Deka:631969,
      author       = {Deka, Dhruba Jyoti and Boro, Bishal and Chen, Yuping and
                      Chahal, Kapil and Nandy, Subhajit and Wang, Caiqi and Lin,
                      Hongfei and Tang, Qing and Mondal, John},
      title        = {{T}yrosinase {E}nzyme-{I}nspired {C}u({I})-{P}orous
                      {O}rganic {P}olymer for {S}elective {O}xidation of
                      {B}iomass-{D}erived 5-{HMF}},
      journal      = {ACS applied materials $\&$ interfaces},
      volume       = {17},
      number       = {25},
      issn         = {1944-8244},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {PUBDB-2025-02084},
      pages        = {36840 - 36854},
      year         = {2025},
      abstract     = {In biobased PET, terephthalic acid (TPA) can be replaced
                      with biobase alternatives like bioderived 5-diformylfuran
                      (DFF). In this work, we have selectively synthesized DFF
                      from the oxidation of 5-hydroxymethylfurfural (HMF) using
                      our tyrosinase enzyme-inspired catalysts vicinal V-Cu-POP
                      and nonvicinal NV-Cu-POP, respectively. Motivated by the
                      oxygenated form of tyrosinase, we introduced binuclear
                      copper(I) moieties into a porous organic polymer to create
                      enzyme-inspired heterogeneous catalysts for the selective
                      oxidation of HMF. V-Cu-POP can effectively activate O$_2$
                      for mild and selective oxidation because the two Cu centers
                      are in close proximity, which is impossible in the case of
                      NV-Cu-POP. For the determination of the coordination
                      environment of the catalytically active site, the X-ray
                      absorption near-edge structure (XANES) studies and the
                      copper(I) state for both the enzyme-inspired catalysts
                      V-Cu-POP and NV-Cu-POP are identified through characteristic
                      features in the absorption spectra. The fitting parameters
                      and EXAFS spectra rule out the formation of the Cu–Cu
                      bond. Further, the key intermediate μ-hydroxy species (Cu
                      (II)–O–O–Cu (II)), which forms during the reaction in
                      the case of the enzyme-inspired catalyst, V-Cu-POP is also
                      confirmed by time-resolved in situ ATR-IR spectroscopy and
                      DFT computational study. This intermediate is not formed in
                      the case of nonvicinal NV-Cu-POP, which is the main reason
                      for lower catalytic activity toward HMF oxidation. NV-Cu-POP
                      still retains the peaks of reactants at the same reaction
                      conditions, which is confirmed by time-resolved in situ
                      ATR-IR spectroscopy. Overall, in this study, we have shown
                      how a tyrosinase enzyme-inspired catalyst exhibits greater
                      catalytic activity toward the oxidation reaction due to the
                      formation of its vicinal conformer compared to the
                      nonvicinal conformer.},
      cin          = {FS-PETRA-S / DOOR ; HAS-User},
      ddc          = {600},
      cid          = {I:(DE-H253)FS-PETRA-S-20210408 /
                      I:(DE-H253)HAS-User-20120731},
      pnm          = {632 - Materials – Quantum, Complex and Functional
                      Materials (POF4-632) / 6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-632 / G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P64-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40512020},
      doi          = {10.1021/acsami.5c09657},
      url          = {https://bib-pubdb1.desy.de/record/631969},
}