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Structure of ADP·AIF4–-stabilized nitrogenase complex and its implications for signal transduction

Author

Listed:
  • Hermann Schindelin

    (California Institute of Technology)

  • Caroline Kisker

    (California Institute of Technology)

  • Jamie L. Schlessman

    (California Institute of Technology)

  • James B. Howard

    (University of Minnesota)

  • Douglas C. Rees

    (California Institute of Technology)

Abstract

The coupling of ATP hydrolysis to electron transfer by the enzyme nitrogenase during biological nitrogen fixation is an important example of a nucleotide-dependent transduction mechanism. The crystal structure has been determined for the complex between the Fe-protein and MoFe-protein components of nitrogenase stabilized by ADP·AIF4–, previously used as a nucleoside triphosphate analogue in nucleotide-switch proteins. The structure reveals that the dimeric Fe-protein has undergone substantial conformational changes. The β-phosphate and AIF4– groups are stabilized through intersubunit contacts that are critical for catalysis and the redox centre is repositioned to facilitate electron transfer. Interactions in the nitrogenase complex have broad implications for signal and energy transduction mechanisms in multiprotein complexes.

Suggested Citation

  • Hermann Schindelin & Caroline Kisker & Jamie L. Schlessman & James B. Howard & Douglas C. Rees, 1997. "Structure of ADP·AIF4–-stabilized nitrogenase complex and its implications for signal transduction," Nature, Nature, vol. 387(6631), pages 370-376, May.
    • Handle: RePEc:nat:nature:v:387:y:1997:i:6631:d:10.1038_387370a0
    DOI: 10.1038/387370a0
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    Cited by:

    1. Yukio Watanabe & Wataru Aoki & Mitsuyoshi Ueda, 2021. "Sustainable Biological Ammonia Production towards a Carbon-Free Society," Sustainability, MDPI, vol. 13(17), pages 1-13, August.

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