•연구자: 화학과 강원철
•발표일: 2023.09
•DOI: https://doi.org/10.14348/molcells.2023.0086
•Wonchull Kang, Molecules and Cells (Q2); Volume 46, Issue 9, Pages 535-537 (2023)
•Abstract
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.