+検索条件
-Structure paper
タイトル | Structural insights into the iron nitrogenase complex. |
---|---|
ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 31, Issue 1, Page 150-158, Year 2024 |
掲載日 | 2023年12月7日 |
![]() | Frederik V Schmidt / Luca Schulz / Jan Zarzycki / Simone Prinz / Niels N Oehlmann / Tobias J Erb / Johannes G Rebelein / ![]() |
PubMed 要旨 | Nitrogenases are best known for catalyzing the reduction of dinitrogen to ammonia at a complex metallic cofactor. Recently, nitrogenases were shown to reduce carbon dioxide (CO) and carbon monoxide ...Nitrogenases are best known for catalyzing the reduction of dinitrogen to ammonia at a complex metallic cofactor. Recently, nitrogenases were shown to reduce carbon dioxide (CO) and carbon monoxide to hydrocarbons, offering a pathway to recycle carbon waste into hydrocarbon products. Among the three nitrogenase isozymes, the iron nitrogenase has the highest wild-type activity for the reduction of CO, but the molecular architecture facilitating these activities has remained unknown. Here, we report a 2.35-Å cryogenic electron microscopy structure of the ADP·AlF-stabilized iron nitrogenase complex from Rhodobacter capsulatus, revealing an [FeSC-(R)-homocitrate] cluster in the active site. The enzyme complex suggests that the iron nitrogenase G subunit is involved in cluster stabilization and substrate channeling and confers specificity between nitrogenase reductase and catalytic component proteins. Moreover, the structure highlights a different interface between the two catalytic halves of the iron and the molybdenum nitrogenase, potentially influencing the intrasubunit 'communication' and thus the nitrogenase mechanism. |
![]() | ![]() ![]() ![]() |
手法 | EM (単粒子) |
解像度 | 2.35 - 2.49 Å |
構造データ | EMDB-16890, PDB-8oie: EMDB-17583, PDB-8pbb: |
化合物 | ![]() ChemComp-S5Q: ![]() ChemComp-HCA: ![]() ChemComp-CLF: ![]() ChemComp-ADP: ![]() ChemComp-MG: ![]() ChemComp-AF3: ![]() ChemComp-SF4: ![]() ChemComp-HOH: |
由来 |
|
![]() | OXIDOREDUCTASE / nitrogen fixation / Fe nitrogenase |