Structural highlights
Function
[NIFD_AZOVI] This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation.
Publication Abstract from PubMed
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.
Structures of the nitrogenase complex prepared under catalytic turnover conditions.,Rutledge HL, Cook BD, Nguyen HPM, Herzik MA Jr, Tezcan FA Science. 2022 Aug 19;377(6608):865-869. doi: 10.1126/science.abq7641. Epub 2022, Jul 28. PMID:35901182[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rutledge HL, Cook BD, Nguyen HPM, Herzik MA Jr, Tezcan FA. Structures of the nitrogenase complex prepared under catalytic turnover conditions. Science. 2022 Aug 19;377(6608):865-869. doi: 10.1126/science.abq7641. Epub 2022, Jul 28. PMID:35901182 doi:http://dx.doi.org/10.1126/science.abq7641
