The complex ATP-Fe2+ serves as a specific affinity cleavage reagent in ATP-Mg2+ sites of Na,K-ATPase: Altered ligation of Fe2+ (Mg2+) ions accompanies the E1Pright-arrowE2P conformational change-Reference-Cited by-同舟云学术

The complex ATP-Fe2+ serves as a specific affinity cleavage reagent in ATP-Mg2+ sites of Na,K-ATPase: Altered ligation of Fe2+ (Mg2+) ions accompanies the E1Pright-arrowE2P conformational change

Published:2000-10-17 Issue:22 Volume:97 Page:11954-11959
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Patchornik G.,Goldshleger R.,Karlish S. J. D.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference36 articles.

1. OCCLUDED CATIONS IN ACTIVE TRANSPORT

2. The Mechanism of Ca2+ Transport by Sarco(Endo)plasmic Reticulum Ca2+-ATPases

3. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution

4. Structural organization, ion transport, and energy transduction of P-type ATPases

5. Structure-function relationships of cation translocation by Ca2+- and Na+,K+-ATPases studied by site-directed mutagenesis

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