Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Article
  • Published:

An efficient catalytic route in haem peroxygenases mediated by O2/small-molecule reductant pairs for sustainable applications

Nature Catalysis volume 8, pages 20–32 (2025)Cite this article

Subjects

Abstract

Haem peroxygenases are attractive biocatalysts for incorporating oxygen into organic molecules using H2O2. However, their practical applications are hindered by irreversible oxidative inactivation due to exogenous H2O2 usage. Here we present an alternative catalytic route in haem peroxygenases that uses O2 and small-molecule reductants such as ascorbic acid and dehydroascorbic acid (DHA) to drive reactions. Our experimental and computational studies indicated that DHAA, the hydrated form of DHA, serves as the key co-substrate that activates oxygen to generate the active oxyferryl haem compound I. We also demonstrate the broad applicability of this O2/reductant-dependent route across various haem peroxygenases, highlighting its biological significance for mono-oxygenase functionality. Importantly, this innovative route avoids the use of H2O2, thereby preventing the risk of irreversible enzyme inactivation. Finally, scaled-up reactions yielded chiral, value-added products with excellent productivity, underscoring the synthetic potential of this developed peroxygenase technology for sustainable chemical transformations.

This is a preview of subscription content, access via your institution

Access options

Buy this article

  • Purchase on SpringerLink
  • Instant access to the full article PDF.

USD 39.95

Prices may be subject to local taxes which are calculated during checkout

Fig. 1: Different catalytic routes of haem-containing oxygenases for generation of Cpd I.
Fig. 2: rAaeUPO-catalysed hydroxylation of 1a in the presence of small-molecule reductants.
Fig. 3: Identification of DHA as the actual co-substrate for rAaeUPO-catalysed reactions.
Fig. 4: Mechanistic study of the O2 activation by UPOs in the presence of DHAA.
Fig. 5: Identification of GA and PA as co-substrates for rAaeUPO-catalysed reactions.
Fig. 6: UPO- and P450-peroxygenase-catalysed oxidative reactions with different reductants.
Fig. 7: rAaeUPO-catalysed conversion of 5a to 5b with O2/reductant- and H2O2-dependent processes.
Fig. 8: Scale-up reactions for preparations of high-value-added products using AscA as a reductant.

Similar content being viewed by others

Data availability

The data that support the findings of this study are available within the main text and its Supplementary Information or from the authors upon reasonable request. Source data are provided with this paper.

References

  1. Sigmund, M. C. & Poelarends, G. J. Current state and future perspectives of engineered and artificial peroxygenases for the oxyfunctionalization of organic molecules. Nat. Catal. 3, 690–702 (2020).

    Article  CAS  Google Scholar 

  2. Hobisch, M. et al. Recent developments in the use of peroxygenases—exploring their high potential in selective oxyfunctionalisations. Biotechnol. Adv. 51, 107615 (2021).

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  3. Kumari, R., Singh, A. & Yadav, A. N. Fungal enzymes: degradation and detoxification of organic and inorganic pollutants. Recent Trends Mycol. Res. 2, 99–125 (2021).

    Google Scholar 

  4. Hanano, A. et al. Plant seed peroxygenase is an original heme-oxygenase with an EF-hand calcium binding motif. J. Biol. Chem. 281, 33140–33151 (2006).

    Article  PubMed  CAS  Google Scholar 

  5. Fuchs, C. & Schwab, W. Epoxidation, hydroxylation and aromatization is catalyzed by a peroxygenase from Solanum lycopersicum. J. Mol. Catal. B 96, 52–60 (2013).

    Article  CAS  Google Scholar 

  6. Podust, L. M. & Sherman, D. H. Diversity of P450 enzymes in the biosynthesis of natural products. Nat. Prod. Rep. 29, 1251–1266 (2012).

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  7. Aratani, Y. Myeloperoxidase: its role for host defense, inflammation, and neutrophil function. Arch. Biochem. Biophys. 640, 47–52 (2018).

    Article  PubMed  CAS  Google Scholar 

  8. Kim, J., Hollmann, F. & Park, C. B. Lignin as a multifunctional photocatalyst for solar powered biocatalytic oxyfunctionalization of C–H bonds. Nat. Synth. 1, 217–226 (2022).

    Article  CAS  Google Scholar 

  9. Grogan, G. Hemoprotein catalyzed oxygenations: P450s, UPOs, and progress toward scalable reactions. JACS Au 1, 1312–1329 (2021).

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  10. Zhang, K. et al. Biocatalytic enantioselective β‐hydroxylation of unactivated C–H bonds in aliphatic carboxylic acids. Angew. Chem. Int. Ed. 61, e202204290 (2022).

    Article  CAS  Google Scholar 

  11. Pickl, M. et al. Mechanistic studies of fatty acid activation by CYP152 peroxygenases reveal unexpected desaturase activity. ACS Catal. 9, 565–577 (2018).

    Article  PubMed  PubMed Central  Google Scholar 

  12. Ramanan, R., Dubey, K. D., Wang, B., Mandal, D. & Shaik, S. Emergence of function in P450-proteins: a combined quantum mechanical/molecular mechanical and molecular dynamics study of the reactive species in the H2O2-dependent cytochrome P450SPα and its regio- and enantioselective hydroxylation of fatty acids. J. Am. Chem. Soc. 138, 6786–6797 (2016).

    Article  PubMed  CAS  Google Scholar 

  13. Jiang, Y. et al. Unexpected reactions of α,β-unsaturated fatty acids provide insight into the mechanisms of CYP152 peroxygenases. Angew. Chem. Int. Ed. 60, 24694–24701 (2021).

    Article  CAS  Google Scholar 

  14. Urlacher, V. B. & Girhard, M. Cytochrome P450 monooxygenases in biotechnology and synthetic biology. Trends Biotechnol. 37, 882–897 (2019).

    Article  PubMed  CAS  Google Scholar 

  15. Li, S., Du, L. & Bernhardt, R. Redox partners: function modulators of bacterial P450 enzymes. Trends Microbiol. 28, 445–454 (2020).

    Article  PubMed  CAS  Google Scholar 

  16. Burek, B. O., Bormann, S., Hollmann, F., Bloh, J. Z. & Holtmann, D. Hydrogen peroxide driven biocatalysis. Green Chem. 21, 3232–3249 (2019).

    Article  CAS  Google Scholar 

  17. Kracher, D. et al. Extracellular electron transfer systems fuel cellulose oxidative degradation. Science 352, 1098–1101 (2016).

    Article  PubMed  CAS  Google Scholar 

  18. Ullrich, R., Nuske, J., Scheibner, K., Spantzel, J. & Hofrichter, M. Novel haloperoxidase from the agaric basidiomycete Agrocybe aegerita oxidizes aryl alcohols and aldehydes. Appl. Environ. Microbiol. 70, 4575–4581 (2004).

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  19. Molina-Espeja, P. et al. Directed evolution of unspecific peroxygenase from Agrocybe aegerita. Appl. Environ. Microbiol. 80, 3496–3507 (2014).

    Article  PubMed  PubMed Central  Google Scholar 

  20. Njus, D., Kelley, P. M., Tu, Y. J. & Schlegel, H. B. Ascorbic acid: the chemistry underlying its antioxidant properties. Free Radic. Biol. Med. 159, 37–43 (2020).

    Article  PubMed  CAS  Google Scholar 

  21. Deutsch, J. C. Dehydroascorbic acid. J. Chromatogra. 881, 299–307 (2000).

    Article  CAS  Google Scholar 

  22. Chebrolu, K. K., Jayaprakasha, G. K., Yoo, K. S., Jifon, J. L. & Patil, B. S. An improved sample preparation method for quantification of ascorbic acid and dehydroascorbic acid by HPLC. LWT Food Sci. Technol. 47, 443–449 (2012).

    Article  CAS  Google Scholar 

  23. Stepnov, A. A. et al. The impact of reductants on the catalytic efficiency of a lytic polysaccharide monooxygenase and the special role of dehydroascorbic acid. FEBS Lett. 596, 53–70 (2022).

    Article  PubMed  CAS  Google Scholar 

  24. Yu, H. S., Zhang, W., Verma, P., He, X. & Truhlar, D. G. Nonseparable exchange-correlation functional for molecules, including homogeneous catalysis involving transition metals. Phys. Chem. Chem. Phys. 17, 12146–12160 (2015).

    Article  PubMed  CAS  Google Scholar 

  25. Zheng, J., Wang, D. & Thiel, W. QM/MM study of mechanisms for compound I formation in the catalytic cycle of cytochrome P450cam. J. Am. Chem. Soc. 128, 13204–13215 (2006).

    Article  PubMed  CAS  Google Scholar 

  26. Derat, E., Shaik, S., Rovira, C., Vidossich, P. & Alfonso-Prieto, M. The effect of a water molecule on the mechanism of formation of compound 0 in horseradish peroxidase. J. Am. Chem. Soc. 129, 6346–6347 (2007).

    Article  PubMed  CAS  Google Scholar 

  27. Vidossich, P. et al. On the role of water in peroxidase catalysis: a theoretical investigation of HRP compound I formation. J. Phys. Chem. B 114, 5161–5169 (2010).

    Article  PubMed  CAS  Google Scholar 

  28. Isaksen et al. A C4-oxidizing lytic polysaccharide monooxygenase cleaving both cellulose and cello-oligosaccharides. J. Biol. Chem. 289, 2632–2642 (2014).

    Article  PubMed  CAS  Google Scholar 

  29. Kittl, R., Kracher, D., Burgstaller, D., Haltrich, D. & Ludwig, R. Production of four Neurospora crassa lytic polysaccharide monooxygenases in Pichia pastoris monitored by a fluorometric assay. Biotechnol. Biofuels 5, 1–14 (2012).

    Article  Google Scholar 

  30. Bissaro, B. et al. Oxidative cleavage of polysaccharides by monocopper enzymes depends on H2O2. Nat. Chem. Biol. 13, 1123–1128 (2017).

    Article  PubMed  CAS  Google Scholar 

  31. Wang, X., Peter, S., Kinne, M., Hofrichter, M. & Groves, J. T. Detection and kinetic characterization of a highly reactive heme-thiolate peroxygenase compound I. J. Am. Chem. Soc. 134, 12897–12900 (2012).

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  32. Rittle, J. & Green, M. T. Cytochrome P450 compound I: capture, characterization, and C–H bond activation kinetics. Science 330, 933–937 (2010).

    Article  PubMed  CAS  Google Scholar 

  33. Wang, B., Zhang, X., Fang, W., Rovira, C. & Shaik, S. How do metalloproteins tame the Fenton reaction and utilize ·OH radicals in constructive manners? Acc. Chem. Res. 55, 2280–2290 (2022).

    Article  PubMed  CAS  Google Scholar 

  34. Tulyathan, V., Boulton, R. B. & Singleton, V. L. Oxygen uptake by gallic acid as a model for similar reactions in wines. J. Agric. Food Chem. 37, 844–849 (1989).

    Article  CAS  Google Scholar 

  35. Grzesik, M. et al. Dietary antioxidants as a source of hydrogen peroxide. Food Chem. 278, 692–699 (2019).

    Article  PubMed  CAS  Google Scholar 

  36. Valderrama, B., Ayala, M. & Vazquez-Duhalt, R. Suicide inactivation of peroxidases and the challenge of engineering more robust enzymes. Chem. Biol. 9, 555–565 (2002).

    Article  PubMed  CAS  Google Scholar 

  37. Carro, J. et al. Modulating fatty acid epoxidation vs hydroxylation in a fungal peroxygenase. ACS Catal. 9, 6234–6242 (2019).

    Article  CAS  Google Scholar 

  38. Getrey, L., Krieg, T., Hollmann, F., Schrader, J. & Holtmann, D. Enzymatic halogenation of the phenolic monoterpenes thymol and carvacrol with chloroperoxidase. Green. Chem. 16, 1104–1108 (2014).

    Article  CAS  Google Scholar 

  39. Karich, A., Scheibner, K., Ullrich, R. & Hofrichter, M. Exploring the catalase activity of unspecific peroxygenases and the mechanism of peroxide-dependent heme destruction. J. Mol. Catal. B 134, 238–246 (2016).

    Article  CAS  Google Scholar 

  40. Wu, F. et al. Quercetagetin alleviates zearalenone-induced liver injury in rabbits through Keap1/Nrf2/ARE signaling pathway. Front Pharm. 14, 1271384 (2023).

    Article  CAS  Google Scholar 

  41. Wu, F. et al. Effects of dietary supplementation with quercetagetin on nutrient digestibility, intestinal morphology, immunity, and antioxidant capacity of broilers. Front. Vet. Sci. 9, 1060140 (2022).

    Article  PubMed  PubMed Central  Google Scholar 

  42. Zhou, Y. et al. Characterization of enzymes specifically producing chiral flavor compounds (R)- and (S)-1-phenylethanol from tea (Camellia sinensis) flowers. Food Chem. 280, 27–33 (2019).

    Article  PubMed  CAS  Google Scholar 

  43. Bertolini, V. et al. Synthesis of α-hydroxy fatty acids from fatty acids by intermediate α-chlorination with TCCA under solvent-free conditions: a way to valorization of waste fat biomasses. ACS Omega 6, 31901–31906 (2021).

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  44. Tonin, F. et al. Pilot-scale production of peroxygenase from Agrocybe aegerita. Org. Process Res. Dev. 25, 1414–1418 (2021).

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  45. Giuriato, D. et al. Design of a H2O2-generating P450SPα fusion protein for high yield fatty acid conversion. Protein Sci. 31, e4501 (2022).

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  46. Qu, G. et al. The crucial role of methodology development in directed evolution of selective enzymes. Angew. Chem. Int. Ed. 59, 13204–13231 (2020).

    Article  CAS  Google Scholar 

  47. Jiang, Y. et al. Biochemical characterization of three new α-olefin-producing P450 fatty acid decarboxylases with a halophilic property. Biotechnol. Biofuels 12, 79 (2019).

    Article  PubMed  PubMed Central  Google Scholar 

  48. Ramirez-Escudero, M. et al. Structural insights into the substrate promiscuity of a laboratory-evolved peroxygenase. ACS Chem. Biol. 13, 3259–3268 (2018).

    Article  PubMed  CAS  Google Scholar 

  49. Sundaramoorthy, M., Terner, J. & Poulosl, T. L. The crystal structure of chloroperoxidase: a heme peroxidase–cytochrome P450 functional hybrid. Structures 3, 1367–1377 (1995).

    Article  CAS  Google Scholar 

  50. Belcher, J. et al. Structure and biochemical properties of the alkene producing cytochrome P450 OleTJE (CYP152L1) from the Jeotgalicoccus sp. 8456 Bacterium. J. Biol. Chem. 289, 6535–6550 (2014).

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  51. Shoji, O. et al. Understanding substrate misrecognition of hydrogen peroxide dependent cytochrome P450 from Bacillus subtilis. J. Biol. Inorg. Chem. 15, 1331–1339 (2010).

    Article  PubMed  CAS  Google Scholar 

  52. Fujishiro, T. et al. Chiral-substrate-assisted stereoselective epoxidation catalyzed by H2O2-dependent cytochrome P450SPα. Chem. Asian J. 7, 2286–2293 (2012).

    Article  PubMed  CAS  Google Scholar 

  53. Søndergaard, C. R., Olsson, M., Rostkowski, M. & Jensen, J. H. Improved treatment of ligands and coupling effects in empirical calculation and rationalization of pKa values. J. Chem. Theory Comput. 7, 2284–2295 (2011).

    Article  PubMed  Google Scholar 

  54. Trott, O. & Olson, A. J. AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J. Comput. Chem. 31, 455–461 (2009).

    Article  Google Scholar 

  55. Pettersen, E. F. et al. UCSF Chimera—a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605–1612 (2004).

    Article  PubMed  CAS  Google Scholar 

  56. Bayly, C. I., Cieplak, P., Cornell, W. D. & Kollman, P. A. A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges: the RESP model. J. Phys. Chem. C 97, 10269–10280 (1993).

    Article  CAS  Google Scholar 

  57. Maier, J. A. et al. ff14SB: improving the accuracy of protein side chain and backbone parameters from ff99SB. J. Chem. Theory Comput. 11, 3696–3713 (2015).

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  58. Li, P. & Merz, K. M. MCPB.py: a Python based metal center parameter builder. J. Chem. Inf. Model. 56, 599–604 (2016).

    Article  PubMed  CAS  Google Scholar 

  59. Li, P. & Merz, K. M. Metal ion modeling using classical mechanics. Chem. Rev. 117, 1564–1686 (2017).

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  60. Izaguirre, J. A., Catarello, D. P., Wozniak, J. M. & Skeel, R. D. Langevin stabilization of molecular dynamics. J. Chem. Phys. 114, 2090–2098 (2001).

    Article  CAS  Google Scholar 

  61. Berendsen, H. J. C., Postma, J. P. M., Gunsteren, W. F., DiNola, A. & Haak, J. R. Molecular dynamics with coupling to an external bath. J. Chem. Phys. 81, 3684–3690 (1984).

    Article  CAS  Google Scholar 

  62. Kräutler, V., Gunsteren, W. F. & Hünenberger, P. H. A fast SHAKE algorithm to solve distance constraint equations for small molecules in molecular dynamics simulations. J. Comput. Chem. 22, 501–508 (2001).

    Article  Google Scholar 

  63. Darden, T., York, D. & Pedersen, L. Particle mesh Ewald: an N⋅log(N) method for Ewald sums in large systems. J. Chem. Phys. 98, 10089–10092 (1993).

    Article  CAS  Google Scholar 

  64. Ylilauri, M. & Pentikäinen, O. T. MMGBSA as a tool to understand the binding affinities of filamin–peptide interactions. J. Chem. Inf. Model. 53, 2626–2633 (2013).

    Article  PubMed  CAS  Google Scholar 

  65. Case, D. A. et al. AMBER 2018 (University of California, 2018).

  66. Lu, Y. et al. Open-source, Python-based redevelopment of the ChemShell multiscale QM/MM environment. J. Chem. Theory Comput. 15, 1317–1328 (2019).

    Article  PubMed  CAS  Google Scholar 

  67. Kästner, J., Carr, J. M., Keal, T. W., Thiel, W. & Wander, A. DL-FIND: an open-source geometry optimizer for atomistic simulations. J. Phys. Chem. A 113, 11856–11865 (2009).

    Article  PubMed  Google Scholar 

  68. Metz, S., Kästner, J., Sokol, A. A., Keal, T. W. & Sherwood, P. ChemShell—a modular software package for QM/MM simulations. WIRES Comput. Mol. Sci. 4, 101–110 (2014).

    Article  CAS  Google Scholar 

  69. Neese, F. The ORCA program system. WIRES Comput. Mol. Sci. 2, 73–78 (2012).

    Article  CAS  Google Scholar 

  70. Neese, F. Software update: the ORCA program system, version 4.0. WIRES Comput. Mol. Sci. 8, e1327 (2018).

    Article  Google Scholar 

  71. Neese, F., Wennmohs, F., Becker, U. & Riplinger, C. The ORCA quantum chemistry program package. J. Chem. Phys. 152, 224108 (2020).

    Article  PubMed  CAS  Google Scholar 

  72. Neese, F. Software update: the ORCA program system—version 5.0. WIRES Comput. Mol. Sci. 12, e1606 (2022).

    Article  Google Scholar 

  73. Helmich-Paris, B., Souza, B., Neese, F. & Izsák, R. An improved chain of spheres for exchange algorithm. J. Chem. Phys. 155, 104109 (2021).

    Article  PubMed  CAS  Google Scholar 

  74. Smith, W., Yong, C. W. & Rodger, P. M. DL_POLY: application to molecular simulation. Mol. Simul. 28, 385–471 (2002).

    Article  CAS  Google Scholar 

  75. Bakowies, D. & Thiel, W. Hybrid models for combined quantum mechanical and molecular mechanical approaches. J. Chem. Phys. 100, 10580–10594 (1996).

    Article  CAS  Google Scholar 

  76. Handy, N. C. & Cohen, A. J. Left–right correlation energy. Mol. Phys. 99, 403–412 (2009).

    Article  Google Scholar 

  77. Lee, C., Yang, W. & Parr, R. G. Development of the Colle–Salvetti correlation-energy formula into a functional of the electron density. Phys. Rev. B 37, 785–789 (1988).

    Article  CAS  Google Scholar 

  78. Billeter, S. R., Turner, A. J. & Thiel, W. Linear scaling geometry optimisation and transition state search in hybrid delocalised internal coordinates. Phys. Chem. Chem. Phys. 2, 2177–2186 (2000).

    Article  CAS  Google Scholar 

  79. Frisch, M. J. et al. Gaussian 16, revision A.03 (Gaussian, 2016).

  80. Becke, A. D. Density-functional thermochemistry. II. The effect of the Perdew–Wang generalized-gradient correlation correction. J. Chem. Phys. 97, 9173–9177 (1992).

    Article  CAS  Google Scholar 

  81. Becke, A. D. Density-functional thermochemistry. III. The role of exact exchange. J. Chem. Phys. 98, 5648–5652 (1993).

    Article  CAS  Google Scholar 

  82. Weigend, F. & Ahlrichs, R. Balanced basis sets of split valence, triple zeta valence and quadruple zeta valence quality for H to Rn: design and assessment of accuracy. Phys. Chem. Chem. Phys. 7, 3297–3305 (2005).

    Article  PubMed  CAS  Google Scholar 

  83. Marenich, A. V., Cramer, C. J. & Truhlar, D. G. Universal solvation model based on solute electron density and on a continuum model of the solvent defined by the bulk dielectric constant and atomic surface tensions. J. Phys. Chem. 113, 6378–6396 (2009).

    Article  CAS  Google Scholar 

  84. Grimme, S., Ehrlich, S. & Goerigk, L. Effect of the damping function in dispersion corrected density functional theory. J. Comput. Chem. 32, 1456–1465 (2011).

    Article  PubMed  CAS  Google Scholar 

  85. Grimme, S. Semiempirical GGA‐type density functional constructed with a long‐range dispersion correction. J. Comput. Chem. 27, 1787–1799 (2006).

    Article  PubMed  CAS  Google Scholar 

Download references

Acknowledgements

This study was supported by the National Key Research and Development Program of China (grant number 2019YFA09005000 (A.L.)), the National Natural Science Foundation of China (grant number 32371552 (A.L.), 22122305 (B.W.)) and the Research Program of State Key Laboratory of Biocatalysis and Enzyme Engineering. We also thank X. Xu and X. Liu for helpful discussions and support.

Author information

Author notes

  1. These authors contributed equally: Di Deng, Zhihui Jiang, Lixin Kang.

Authors and Affiliations

  1. State Key Laboratory of Biocatalysis and Enzyme Engineering, Hubei Key Laboratory of Industrial Biotechnology, School of Life Sciences, Hubei University, Wuhan, P. R. China

    Di Deng, Lixin Kang, Xiaodong Zhang, Yuben Qiao & Aitao Li

  2. State Key Laboratory of Physical Chemistry of Solid Surfaces and Fujian Provincial Key Laboratory of Theoretical and Computational Chemistry, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen, P. R. China

    Zhihui Jiang, Langxing Liao, Yang Zhou, Liulin Yang & Binju Wang

Authors
  1. Di Deng
    View author publications

    Search author on:PubMed Google Scholar

  2. Zhihui Jiang
    View author publications

    Search author on:PubMed Google Scholar

  3. Lixin Kang
    View author publications

    Search author on:PubMed Google Scholar

  4. Langxing Liao
    View author publications

    Search author on:PubMed Google Scholar

  5. Xiaodong Zhang
    View author publications

    Search author on:PubMed Google Scholar

  6. Yuben Qiao
    View author publications

    Search author on:PubMed Google Scholar

  7. Yang Zhou
    View author publications

    Search author on:PubMed Google Scholar

  8. Liulin Yang
    View author publications

    Search author on:PubMed Google Scholar

  9. Binju Wang
    View author publications

    Search author on:PubMed Google Scholar

  10. Aitao Li
    View author publications

    Search author on:PubMed Google Scholar

Contributions

A.L. and B.W. conceived and supervised the project. D.D., Z.J., L.K., L.L., X.Z., Y.Q., Y.Z. and L.Y. performed the experiments and analysed the data. A.L., B.W., D.D. and Z.J. wrote the manuscript. All authors checked and modified the manuscript.

Corresponding authors

Correspondence to Binju Wang or Aitao Li.

Ethics declarations

Competing interests

The authors declare no competing interests.

Peer review

Peer review information

Nature Catalysis thanks Martin Hayes and the other, anonymous, reviewer(s) for their contribution to the peer review of this work.

Additional information

Publisher’s note Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Supplementary information

Supplementary Information (download PDF )

Supplementary Methods, Tables 1–7 and Figs. 1–31.

Reporting Summary (download PDF )

Supplementary Data 1 (download XLSX )

Source data for Supplementary Figs. 9, 12–14, 17.

Supplementary Data 2 (download ZIP )

Initial and final structures in molecular dynamics simulations.

Supplementary Data 3 (download TXT )

The atomic coordinates of the optimized computational models.

Source data

Source Data Figs. 2, 3, 5–8 (download XLSX )

Statistical source data for Figs. 2, 3, 5–8.

Rights and permissions

Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Deng, D., Jiang, Z., Kang, L. et al. An efficient catalytic route in haem peroxygenases mediated by O2/small-molecule reductant pairs for sustainable applications. Nat Catal 8, 20–32 (2025). https://doi.org/10.1038/s41929-024-01281-7

Download citation

  • Received:

  • Accepted:

  • Published:

  • Version of record:

  • Issue date:

  • DOI: https://doi.org/10.1038/s41929-024-01281-7

This article is cited by

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing