Study of ATP binding in the active site of Na+,K+‐ATPase as probed by ultraviolet resonance Raman spectroscopy

FEBS Letters

Feofanov, A.V.¹  Modyanov, N.N.¹  Dzhandzhugazyan, K.N.¹  Nabiev, I.R.¹  Efremov, R.G.¹ 

[1] Shemyakin Institute of Bioorganic Chemistry, USSR Academy of Sciences, Ul. Miklukho-Maklaya, 16/10, 117871, Moscow V-437, USSR

关键词: Na+K+-ATPase;    ATP;    Raman spectroscopy;    Ultraviolet resonance Raman spectroscopy;   

DOI  :  10.1016/0014-5793(90)80117-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown