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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...
Tallennettuna:
| Julkaisussa: | Front Microbiol |
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| Päätekijät: | , , , , , , , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
Frontiers Media S.A.
2019
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| Aiheet: | |
| Linkit: | 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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