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Deciphering the assembly process of PQQ dependent methanol dehydrogenase

Author

Listed:
  • Haichuan Zhou

    (Chinese Academy of Sciences
    National Center of Technology Innovation for Synthetic Biology)

  • Junqing Sun

    (Zhejiang University School of Medicine
    Shanxi Academy of Advanced Research and Innovation)

  • Jian Cheng

    (Chinese Academy of Sciences
    National Center of Technology Innovation for Synthetic Biology)

  • Min Wu

    (Chinese Academy of Sciences
    National Center of Technology Innovation for Synthetic Biology)

  • Jie Bai

    (Chinese Academy of Sciences
    National Center of Technology Innovation for Synthetic Biology)

  • Qian Li

    (Chinese Academy of Sciences
    National Center of Technology Innovation for Synthetic Biology)

  • Jie Shen

    (Chinese Academy of Sciences
    National Center of Technology Innovation for Synthetic Biology)

  • Manman Han

    (Chinese Academy of Sciences
    National Center of Technology Innovation for Synthetic Biology)

  • Chen Yang

    (Chinese Academy of Sciences
    National Center of Technology Innovation for Synthetic Biology)

  • Liangpo Li

    (Chinese Academy of Sciences
    National Center of Technology Innovation for Synthetic Biology)

  • Yuwan Liu

    (Chinese Academy of Sciences
    National Center of Technology Innovation for Synthetic Biology)

  • Qichen Cao

    (Chinese Academy of Sciences
    National Center of Technology Innovation for Synthetic Biology)

  • Weidong Liu

    (Chinese Academy of Sciences
    National Center of Technology Innovation for Synthetic Biology)

  • Haixia Xiao

    (Chinese Academy of Sciences)

  • Hongjun Dong

    (Chinese Academy of Sciences
    National Center of Technology Innovation for Synthetic Biology)

  • Feng Gao

    (Chinese Academy of Sciences)

  • Huifeng Jiang

    (Chinese Academy of Sciences
    National Center of Technology Innovation for Synthetic Biology
    Zhejiang A&F University)

Abstract

Pyrroloquinoline quinone (PQQ)-dependent methanol dehydrogenases (MDHs), the periplasmic metalloenzymes in Gram-negative methylotrophic bacteria, play a pivotal role in methane and methanol bio-utilization. Although the structures of many PQQ-dependent MDHs have been resolved, including the canonical heterotetrameric enzymes composed of two MxaF and two MxaI subunits with a molecule of PQQ and a calcium ion in the active site in MxaF, the biogenesis of these enzymes remains elusive. Here, we characterize a chaperone, MxaJ, responsible for PQQ incorporation by reconstructing a PQQ-dependent MDH assembly system in Escherichia coli. Using cryo-electron microscopy, we capture the structures of the intermediate complexes formed by the chaperone MxaJ and catalytic subunit MxaF during PQQ-dependent MDH maturation, revealing a chaperone-mediated molecular mechanism of cofactor incorporation. These findings not only advance our understanding on the biogenesis of PQQ-dependent MDH, but also provide an alternative engineering way for methane and methanol bioconversion.

Suggested Citation

  • Haichuan Zhou & Junqing Sun & Jian Cheng & Min Wu & Jie Bai & Qian Li & Jie Shen & Manman Han & Chen Yang & Liangpo Li & Yuwan Liu & Qichen Cao & Weidong Liu & Haixia Xiao & Hongjun Dong & Feng Gao & , 2025. "Deciphering the assembly process of PQQ dependent methanol dehydrogenase," Nature Communications, Nature, vol. 16(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-61958-w
    DOI: 10.1038/s41467-025-61958-w
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