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Probing the coordination and function of Fe4S4 modules in nitrogenase assembly protein NifB

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Listed:
  • Lee A. Rettberg

    (University of California)

  • Jarett Wilcoxen

    (University of California)

  • Chi Chung Lee

    (University of California)

  • Martin T. Stiebritz

    (University of California)

  • Kazuki Tanifuji

    (University of California)

  • R. David Britt

    (University of California)

  • Yilin Hu

    (University of California)

Abstract

NifB is an essential radical S-adenosylmethionine (SAM) enzyme for nitrogenase cofactor assembly. Previous studies show that NifB couples a putative pair of [Fe4S4] modules (designated K1 and K2) into an [Fe8S9C] cofactor precursor concomitant with radical SAM-dependent carbide insertion through the action of its SAM-binding [Fe4S4] module. However, the coordination and function of the NifB cluster modules remain unknown. Here, we use continuous wave and pulse electron paramagnetic resonance spectroscopy to show that K1- and K2-modules are 3-cysteine-coordinated [Fe4S4] clusters, with a histidine-derived nitrogen serving as the fourth ligand to K1 that is lost upon K1/K2-coupling. Further, we demonstrate that coexistence of SAM/K2-modules is a prerequisite for methyltransfer to K2 and hydrogen abstraction from the K2-associated methyl by a 5′-deoxyadenosyl radical. These results establish an important framework for mechanistic explorations of NifB while highlighting the utility of a synthetic-cluster-based reconstitution approach employed herein in functional analyses of iron–sulfur (FeS) enzymes.

Suggested Citation

  • Lee A. Rettberg & Jarett Wilcoxen & Chi Chung Lee & Martin T. Stiebritz & Kazuki Tanifuji & R. David Britt & Yilin Hu, 2018. "Probing the coordination and function of Fe4S4 modules in nitrogenase assembly protein NifB," Nature Communications, Nature, vol. 9(1), pages 1-8, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-05272-8
    DOI: 10.1038/s41467-018-05272-8
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