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Structural consequences of turnover-induced homocitrate loss in nitrogenase

Author

Listed:
  • Rebeccah A. Warmack

    (California Institute of Technology)

  • Ailiena O. Maggiolo

    (California Institute of Technology)

  • Andres Orta

    (California Institute of Technology)

  • Belinda B. Wenke

    (California Institute of Technology)

  • James B. Howard

    (University of Minnesota)

  • Douglas C. Rees

    (California Institute of Technology
    California Institute of Technology)

Abstract

Nitrogenase catalyzes the ATP-dependent reduction of dinitrogen to ammonia during the process of biological nitrogen fixation that is essential for sustaining life. The active site FeMo-cofactor contains a [7Fe:1Mo:9S:1C] metallocluster coordinated with an R-homocitrate (HCA) molecule. Here, we establish through single particle cryoEM and chemical analysis of two forms of the Azotobacter vinelandii MoFe-protein – a high pH turnover inactivated species and a ∆NifV variant that cannot synthesize HCA – that loss of HCA is coupled to α-subunit domain and FeMo-cofactor disordering, and formation of a histidine coordination site. We further find a population of the ∆NifV variant complexed to an endogenous protein identified through structural and proteomic approaches as the uncharacterized protein NafT. Recognition by endogenous NafT demonstrates the physiological relevance of the HCA-compromised form, perhaps for cofactor insertion or repair. Our results point towards a dynamic active site in which HCA plays a role in enabling nitrogenase catalysis by facilitating activation of the FeMo-cofactor from a relatively stable form to a state capable of reducing dinitrogen under ambient conditions.

Suggested Citation

  • Rebeccah A. Warmack & Ailiena O. Maggiolo & Andres Orta & Belinda B. Wenke & James B. Howard & Douglas C. Rees, 2023. "Structural consequences of turnover-induced homocitrate loss in nitrogenase," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
  • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-36636-4
    DOI: 10.1038/s41467-023-36636-4
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    References listed on IDEAS

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    1. Yun-Tao Liu & Heng Zhang & Hui Wang & Chang-Lu Tao & Guo-Qiang Bi & Z. Hong Zhou, 2022. "Isotropic reconstruction for electron tomography with deep learning," Nature Communications, Nature, vol. 13(1), pages 1-17, December.
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    3. Ka Man Yip & Niels Fischer & Elham Paknia & Ashwin Chari & Holger Stark, 2020. "Atomic-resolution protein structure determination by cryo-EM," Nature, Nature, vol. 587(7832), pages 157-161, November.
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