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The complex ATP–Fe(2+) serves as a specific affinity cleavage reagent in ATP-Mg(2+) sites of Na,K-ATPase: Altered ligation of Fe(2+) (Mg(2+)) ions accompanies the E(1)P→E(2)P conformational change

In the presence of ascorbate/H(2)O(2), ATP–Fe(2+) or AMP-PNP–Fe(2+) complexes act as affinity cleavage reagents, mediating selective cleavage of the alpha subunit of Na,K-ATPase at high affinity ATP–Mg(2+) sites. The cleavages reveal contact points of Fe(2+) or Mg(2+) ions. In E(1) and E(1)Na confor...

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書目詳細資料
發表在:Proc Natl Acad Sci U S A
Principais autores: Patchornik, Guy, Goldshleger, Rivka, Karlish, Steven J. D.
格式: Artigo
語言:Inglês
出版: National Academy of Sciences 2000
主題:
在線閱讀:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC17276/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/11035801/
https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.220332897
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