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Unveiling Nature's Nitrogen-Fixing Secrets

Molecules and Cells, 2023, 46(9), , pp.535-537 [Peer Reviewed Journal]

The Korean Society for Molecular and Cellular Biology. All rights reserved. 2023 ;ISSN: 1016-8478 ;EISSN: 0219-1032 ;DOI: 10.14348/molcells.2023.0086 ;PMID: 37691259

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  • Title:
    Unveiling Nature's Nitrogen-Fixing Secrets
  • Author: Kang, Wonchull
  • Subjects: Journal Club ; 생물학
  • Is Part Of: Molecules and Cells, 2023, 46(9), , pp.535-537
  • Description: Biological nitrogen fixation is the process of converting atmospheric nitrogen to ammonia. This process is catalyzed by a metalloenzyme complex composed of an iron protein (Fe Protein) and an iron-molybdenum protein (MoFe Protein). During adenine triphosphate hydrolysis, electrons are transported from FeP to MoFeP, resulting in the formation a transient nitrogenase complex. Despite its significance, the atomic details of the mechanism remain unknown. In a recent study by Rutledge et al. (2022), who presented the first cryo-electron microscopy structure of the nitrogenase complex, a significant breakthrough was achieved in understanding the structure of the nitrogenase complex structure. The study revealed that one FeP binds to MoFeP, suggesting a ping-pong mechanism. This investigation lays the groundwork for future studies on the structure and mechanism of metalloprotein, particularly nitrogenase. Future research on nitrogenase will provide valuable insights into fundamental biological processes and the advancement of sustainable agricultural practices. ATP, adenosine triphosphate; ADP, adenosine diphosphate. KCI Citation Count: 0
  • Publisher: United States: Korean Society for Molecular and Cellular Biology
  • Language: English;Korean
  • Identifier: ISSN: 1016-8478
    EISSN: 0219-1032
    DOI: 10.14348/molcells.2023.0086
    PMID: 37691259
  • Source: Freely Accessible Journals
    PubMed Central
    Alma/SFX Local Collection
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