Study of ATP binding in the active site of Na+,K+‐ATPase as probed by ultraviolet resonance Raman spectroscopy
- 29 January 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 260 (2) , 257-260
- https://doi.org/10.1016/0014-5793(90)80117-2
Abstract
The ultraviolet resonance Raman (UV RR) spectra of functional ATP/membrane‐bound Na+K+‐ATPase complexes have been obtained. The substrate binding in the enzyme active site has been shown to be accompanied with significant changes in the electronic vibrational structure of the adenine ring. From the spectral analysis of ATP, 8‐Br‐ATP and 6‐NHMe‐adenine at various pH values the conclusion was made that N1 and the NH2, group and, probably, N7 of the substrate adenine part, interact with the protein surroundings via hydrogen bonds.Keywords
This publication has 9 references indexed in Scilit:
- Structure and Function of Plasma Membrane ATPaseAnnual Review of Plant Biology, 1989
- Nuclear Overhauser effect studies of the conformation of Co(NH3)4ATP bound to kidney sodium-potassium ATPaseBiochemistry, 1989
- An ultraviolet resonance Raman study of dehydrogenase enzymes and their interactions with coenzymes and substratesBiochemistry, 1989
- Binding of monovalent cations induces large changes in the secondary structure of Na+,K+‐ATPase as probed by Raman spectroscopyFEBS Letters, 1988
- Differentiated analysis of the secondary structure of hydrophilic and hydrophobic regions in α- and β-subunits of Na+,K+-ATPase by Raman spectroscopyFEBS Letters, 1988
- The pH-dependent laser Raman spectroscopic study of 8-Br-5'AMPJournal of the American Chemical Society, 1987
- The poly dA strand of poly dA.poly dT adopts an A-form in solution: a UV resonance Raman studyNucleic Acids Research, 1985
- ATP binding to solubilized (Na+ + K+)-ATPaseBiochimica et Biophysica Acta (BBA) - Biomembranes, 1983
- Structure and Mechanism of the (Na,K)-ATPasePublished by Elsevier ,1981