α-Lys(424) Participates in Insertion of FeMoco to MoFe Protein and Maintains Nitrogenase Activity in Klebsiella oxytoca M5al

Our previous investigation of substrates reduction catalyzed by nitrogenase suggested that α-Ile(423) of MoFe protein possibly functions as an electron transfer gate to Mo site of active center-“FeMoco”. Amino acid residue α-Lys(424) connects directly to α-Ile(423), and they are located in the same...

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Vydáno v:Front Microbiol
Hlavní autoři: Song, Lina, Liu, Pengxi, Jiang, Wei, Guo, Qingjuan, Zhang, Chunxi, Basit, Abdul, Li, Ying, Li, Jilun
Médium: Artigo
Jazyk:Inglês
Vydáno: Frontiers Media S.A. 2019
Témata:
Microbiology
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC6477116/
https://ncbi.nlm.nih.gov/pubmed/31057512
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.3389/fmicb.2019.00802
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