Quenching of 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole-modified Na+/K+-ATPase reveals a higher accessibility of the low-affinity ATP-binding site
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(97)01460-9/fullpdf
Reference19 articles.
1. Na+/K+-ATPase with a Blocked E1ATP Site Still Allows Backdoor Phosphorylation of the E2ATP site
2. Modification of the E1ATP binding site of Na+/K+-ATPase by the chromium complex of adenosine 5'-[beta,gamma-methylene]triphosphate blocks the overall reaction but not the partial activities of the E2 conformation
3. Low affinity superphosphorylation of the Na,K-ATPase by ATP.
4. Phosphate binding and ATP-binding sites coexist in Na+/K+-transporting ATPase, as demonstrated by the inactivating MgPO4 complex analogue Co(NH3)4PO4
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