Structures of the Nitrogenase Complex Prepared Under Catalytic Turnover Conditions

The enzyme nitrogenase couples adenosine triphosphate (ATP) hydrolysis to the multielectron reduction of atmospheric dinitrogen into ammonia. Despite extensive research, the mechanistic details of ATP-dependent energy transduction and dinitrogen reduction by nitrogenase are not well understood, requ...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2022-08, Vol.377 (6608), p.865-869
Main Authors: Rutledge, Hannah L., Cook, Brian D., Nguyen, Hoang P. M., Jr, Mark A. Herzik, Tezcan, F. Akif
Format: Article
Language:English
Subjects:
Adenosine Triphosphate - chemistry
ATP
Catalysis
Chemistry and Materials (General)
Cryoelectron Microscopy
Crystallography
Crystals
Dithionite
Electron microscopy
Hydrolysis
Molybdoferredoxin - chemistry
Nitrogen fixation
Nitrogenase
Nitrogenase - chemistry
Nitrogenation
Oxidation-Reduction
Protein Conformation
Proteins
Reducing agents
X-ray crystallography
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Summary:The enzyme nitrogenase couples adenosine triphosphate (ATP) hydrolysis to the multielectron reduction of atmospheric dinitrogen into ammonia. Despite extensive research, the mechanistic details of ATP-dependent energy transduction and dinitrogen reduction by nitrogenase are not well understood, requiring new strategies to monitor its structural dynamics during catalytic action. Here, we report cryo–electron microscopy structures of the nitrogenase complex prepared under enzymatic turnover conditions. We observe that asymmetry governs all aspects of the nitrogenase mechanism, including ATP hydrolysis, protein-protein interactions, and catalysis. Conformational changes near the catalytic iron-molybdenum cofactor are correlated with the nucleotide-hydrolysis state of the enzyme.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.abq7641