大连大学学报
大連大學學報
대련대학학보
JOURNAL OF DALIAN UNIVERSITY
2014年
3期
77-81
,共5页
唐乾%张越%曹洪玉%郑学仿
唐乾%張越%曹洪玉%鄭學倣
당건%장월%조홍옥%정학방
血红蛋白%亚硝酸钠%配合物%光谱法
血紅蛋白%亞硝痠鈉%配閤物%光譜法
혈홍단백%아초산납%배합물%광보법
hemoglobin%HbNO%sodium nitrite%spectrometry
采用紫外-可见光谱、荧光光谱、同步荧光光谱和圆二色(CD)光谱等方法研究了人血红蛋白与亚硝酸钠配位反应的光谱学性质。结果表明:血红蛋白与亚硝酸钠配位反应的进行受血红素中心铁原子价态的影响。高铁血红蛋白与亚硝酸钠发生配位反应生成Hb(III)-NaNO2;亚铁血红蛋白与亚硝酸钠反应生成Hb(II)-NaNO2。但是随着时间的推移,Hb(II)-NaNO2配合物逐渐解离,解离出的亚铁血红蛋白逐渐被氧化成高铁血红蛋白,溶液中的亚硝酸钠再与高铁血红蛋白反应,最终生成Hb(III)-NaNO2配合物。此外,荧光光谱、同步荧光光谱和CD数据显示亚硝酸钠的加入改变了血红蛋白氨基酸残基的微环境,且作用点更接近于色氨酸残基位置,而对蛋白质二级结构影响甚微。
採用紫外-可見光譜、熒光光譜、同步熒光光譜和圓二色(CD)光譜等方法研究瞭人血紅蛋白與亞硝痠鈉配位反應的光譜學性質。結果錶明:血紅蛋白與亞硝痠鈉配位反應的進行受血紅素中心鐵原子價態的影響。高鐵血紅蛋白與亞硝痠鈉髮生配位反應生成Hb(III)-NaNO2;亞鐵血紅蛋白與亞硝痠鈉反應生成Hb(II)-NaNO2。但是隨著時間的推移,Hb(II)-NaNO2配閤物逐漸解離,解離齣的亞鐵血紅蛋白逐漸被氧化成高鐵血紅蛋白,溶液中的亞硝痠鈉再與高鐵血紅蛋白反應,最終生成Hb(III)-NaNO2配閤物。此外,熒光光譜、同步熒光光譜和CD數據顯示亞硝痠鈉的加入改變瞭血紅蛋白氨基痠殘基的微環境,且作用點更接近于色氨痠殘基位置,而對蛋白質二級結構影響甚微。
채용자외-가견광보、형광광보、동보형광광보화원이색(CD)광보등방법연구료인혈홍단백여아초산납배위반응적광보학성질。결과표명:혈홍단백여아초산납배위반응적진행수혈홍소중심철원자개태적영향。고철혈홍단백여아초산납발생배위반응생성Hb(III)-NaNO2;아철혈홍단백여아초산납반응생성Hb(II)-NaNO2。단시수착시간적추이,Hb(II)-NaNO2배합물축점해리,해리출적아철혈홍단백축점피양화성고철혈홍단백,용액중적아초산납재여고철혈홍단백반응,최종생성Hb(III)-NaNO2배합물。차외,형광광보、동보형광광보화CD수거현시아초산납적가입개변료혈홍단백안기산잔기적미배경,차작용점경접근우색안산잔기위치,이대단백질이급결구영향심미。
The spectroscopic propertises of reaction between hemoglobin and sodium nitrite were investigated by using UV-Vis absorption spectra, fluorescence spectra, synchronous fluorescence spectra and circular dichroism (CD) spectroscopies. The experimental results showed that the coordination reaction between hemoglobin and sodium nitrite related to the center of heme iron atom valence. Hb(III) reacted with sodium nitrite generating Hb(III)-NaNO2 and Hb(II)NO reacted with sodium nitrite generating Hb(II)-NaNO2. As time went on,Hb(II)-NaNO2 dissociated, and then Hb(II) was oxidized gradually to Hb(III), sodium nitrite reacted with it and generated Hb(III)-NaNO2 in the end. Fluorescence spectrum, synchronous fluorescence spectrum and CD dates all revealed that sodium nitrite changed the microenvironment of Hb amino acid residues, Hb-NaNO2 sites were closer to Try residues, and nearly had no effect on the secondary structure of protein.