Temperature dependence of the rates of conformational changes reported by fluorescein 5'-isothiocyanate modification of the hydrogen ion-potassium- and sodium-potassium-ATPases-Reference-Cited by-同舟云学术

Temperature dependence of the rates of conformational changes reported by fluorescein 5'-isothiocyanate modification of the hydrogen ion-potassium- and sodium-potassium-ATPases

Published:1991-04 Issue:14 Volume:30 Page:3503-3510
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Faller Larry D.,Diaz Ruben A.,Scheiner-Bobis Georgios,Farley Robert A.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00228a022

Reference35 articles.

1. Bioenergetic coupling to protonmotive force: should we be considering hydronium ion coordination and not group protonation?

2. Structure and Mechanism of the (Na,K)-ATPase

3. A characterization of vanadate interactions with the (Na,K)-ATPase. Mechanistic and regulatory implications.

4. The active site structure of Na+- and K+-stimulated ATPase. Location of a specific fluorescein isothiocyanate reactive site.

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