1H‐NMR study of the interaction of aminopyrine with purified rat liver microsomal cytochrome P‐450

FEBS Letters

Woldman, Ya.Yu.²  Lyakhovich, V.V.¹  Gulyaeva, L.F.¹  Weiner, L.M.² 

[1] Institute of Clinical and Experimental Medicine, Novosibirsk 630091, USSR;Institute of Chemical Kinetics and Combustion, Novosibirsk 630090 USSR

关键词: Cytochrome P-450;    Aminopyrine;    1H-NMR;    Enzyme-substrate interaction;    Fe3+-proton distance;    AP;    aminopyrine;    cyt;    cytochrome;    KPi;    potassium phosphate buffer;   

DOI  :  10.1016/0014-5793(85)80279-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Longitudinal relaxation (T ₁) measurements for all lines (N(CH₃)₂, N(CH₃), (C(CH₃), phenyl) in the aminopyrine ¹H-NMR spectrum were used to study the interaction of aminopyrine with purified microsomal cytochrome P-450 from livers of phenobarbital-treated rats. The paramagnetic contribution to the observed t ₁ ⁻¹ values was determined from its dependence on aminopyrine concentration. The Solomon-Bloembergen equation was used to calculate between Fe³⁺ and aminopyrine distances in the enzyme-substrate complex. For all protons these distances are about 8 Å.

【 授权许可】

Unknown