Academic Journal

Chimeric interaction of nitrogenase‐like reductases with the MoFe protein of nitrogenase

التفاصيل البيبلوغرافية
العنوان: Chimeric interaction of nitrogenase‐like reductases with the MoFe protein of nitrogenase
المؤلفون: Jasper, Jan, Ramos, José V., Trncik, Christian, Jahn, Dieter, Einsle, Oliver, Layer, Gunhild, Moser, Jürgen
المصدر: ChemBioChem. - 21, 12 (2020) , 1733-1741, ISSN: 1439-7633
سنة النشر: 2020
المجموعة: University of Freiburg: FreiDok
الوصف: The engineering of transgenic organisms with the ability to fix nitrogen is an attractive possibility. However, oxygen sensitivity of nitrogenase, mainly conferred by the reductase component (NifH)2, is an imminent problem. Nitrogenase-like enzymes involved in coenzyme F430 and chlorophyll biosynthesis utilize the highly homologous reductases (CfbC)2 and (ChlL)2, respectively. Chimeric protein–protein interactions of these reductases with the catalytic component of nitrogenase (MoFe protein) did not support nitrogenase activity. Nucleotide-dependent association and dissociation of these complexes was investigated, but (CfbC)2 and wild-type (ChlL)2 showed no modulation of the binding affinity. By contrast, the interaction between the (ChlL)2 mutant Y127S and the MoFe protein was markedly increased in the presence of ATP (or ATP analogues) and reduced in the ADP state. Upon formation of the octameric (ChlL)2MoFe(ChlL)2 complex, the ATPase activity of this variant is triggered, as seen in the homologous nitrogenase system. Thus, the described reductase(s) might be an attractive tool for further elucidation of the diverse functions of (NifH)2 and the rational design of a more robust reductase.
نوع الوثيقة: article in journal/newspaper
وصف الملف: pdf
اللغة: English
Relation: https://freidok.uni-freiburg.de/data/220404
DOI: 10.1002/cbic.201900759
الاتاحة: https://freidok.uni-freiburg.de/data/220404
https://nbn-resolving.org/urn:nbn:de:bsz:25-freidok-2204049
https://doi.org/10.1002/cbic.201900759
https://freidok.uni-freiburg.de/dnb/download/220404
Rights: free
رقم الانضمام: edsbas.957B6942
قاعدة البيانات: BASE