National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R01GM099813
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R35GM138206
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
T32 GM008326
米国
National Aeronautic Space Administration (NASA, United States)
80NSSC18M0093
米国
引用
ジャーナル: Science / 年: 2022 タイトル: Structures of the nitrogenase complex prepared under catalytic turnover conditions. 著者: Hannah L Rutledge / Brian D Cook / Hoang P M Nguyen / Mark A Herzik / F Akif Tezcan / 要旨: The enzyme nitrogenase couples adenosine triphosphate (ATP) hydrolysis to the multielectron reduction of atmospheric dinitrogen into ammonia. Despite extensive research, the mechanistic details of ...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.