التفاصيل البيبلوغرافية
| العنوان: |
Probing the coordination and function of Fe4S4modules in nitrogenase assembly protein NifB |
| المؤلفون: |
Rettberg, LA, Wilcoxen, J, Lee, CC, Stiebritz, MT, Tanifuji, K, Britt, RD, Hu, Y |
| المصدر: |
Rettberg, LA; Wilcoxen, J; Lee, CC; Stiebritz, MT; Tanifuji, K; Britt, RD; et al.(2018). Probing the coordination and function of Fe4S4modules in nitrogenase assembly protein NifB. Nature Communications, 9(1). doi: 10.1038/s41467-018-05272-8. UC Davis: Retrieved from: http://www.escholarship.org/uc/item/9xb0t2jt |
| بيانات النشر: |
eScholarship, University of California, 2018. |
| سنة النشر: |
2018 |
| الوصف: |
© 2018, The Author(s). NifB is an essential radical S-adenosylmethionine (SAM) enzyme for nitrogenase cofactor assembly. Previous studies show that NifB couples a putative pair of [Fe4S4] modules (designated K1 and K2) into an [Fe8S9C] cofactor precursor concomitant with radical SAM-dependent carbide insertion through the action of its SAM-binding [Fe4S4] module. However, the coordination and function of the NifB cluster modules remain unknown. Here, we use continuous wave and pulse electron paramagnetic resonance spectroscopy to show that K1- and K2-modules are 3-cysteine-coordinated [Fe4S4] clusters, with a histidine-derived nitrogen serving as the fourth ligand to K1 that is lost upon K1/K2-coupling. Further, we demonstrate that coexistence of SAM/K2-modules is a prerequisite for methyltransfer to K2 and hydrogen abstraction from the K2-associated methyl by a 5′-deoxyadenosyl radical. These results establish an important framework for mechanistic explorations of NifB while highlighting the utility of a synthetic-cluster-based reconstitution approach employed herein in functional analyses of iron–sulfur (FeS) enzymes. |
| وصف الملف: |
application/pdf |
| اللغة: |
English |
| URL الوصول: |
https://explore.openaire.eu/search/publication?articleId=od_______325::0c0919470e4815031b4556d25916bb52
http://www.escholarship.org/uc/item/9xb0t2jt |
| حقوق: |
OPEN |
| رقم الأكسشن: |
edsair.od.......325..0c0919470e4815031b4556d25916bb52 |
| قاعدة البيانات: |
OpenAIRE |
