期刊
SCIENCE
卷 377, 期 6608, 页码 865-869出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.abq7641
关键词
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资金
- NIH [R01-GM099813, R35-GM138206, T32-GM008326]
- NASA [80NSSC18M0093]
- Searle Scholars Program
- NIH Common Fund Transformative High-Resolution Cryoelectron Microscopy program [U24 GM129541]
This study reports cryo-electron microscopy structures of the nitrogenase complex prepared under enzymatic turnover conditions. The research reveals that asymmetry plays a critical role in various aspects of the nitrogenase mechanism.
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.
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