α-Lys424 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-Ile423 of MoFe protein possibly functions as an electron transfer gate to Mo site of active center-“FeMoco”. Amino acid residue α-Lys424 connects directly to α-Ile423, and they are located in the same α-heli...

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Hlavní autoři:	Lina Song, Pengxi Liu, Wei Jiang, Qingjuan Guo, Chunxi Zhang, Abdul Basit, Ying Li, Jilun Li
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	Frontiers Media S.A. 2019-04-01
Edice:	Frontiers in Microbiology
Témata:	Klebsiella oxytoca nitrogenase MoFe protein α-Lys424 FeMoco
On-line přístup:	https://www.frontiersin.org/article/10.3389/fmicb.2019.00802/full
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