期刊文献+
共找到1篇文章
< 1 >
每页显示 20 50 100
NMR double resonance study of azide binding to cytochrome c
1
作者 concar D. +3 位作者 MOORE G.R. WILLIAMS R.J.P. 《Chinese Journal of Chemistry》 SCIE CAS CSCD 1992年第1期40-44,共0页
Equilibrium constants for the binding of azide to ferri-cytochrome c at temperature range of 305—325 K were determined at pH=7 by using ~1H double resonance method.Thermodynamic values(⊿H^o=-34.5 kJ/mol,⊿S^o=-100 J... Equilibrium constants for the binding of azide to ferri-cytochrome c at temperature range of 305—325 K were determined at pH=7 by using ~1H double resonance method.Thermodynamic values(⊿H^o=-34.5 kJ/mol,⊿S^o=-100 J/mol)were obtained from van't Hoff's relation and were compared with those for azide binding to other ferric hemeproteins.The reason of lower affinity of cytochrome c for azide was discussed. 展开更多
全文增补中
上一页 1 下一页 到第
使用帮助 返回顶部