一种用于表征六配位血红蛋白动力学的闪光光解方法。
A flash photolysis method to characterize hexacoordinate hemoglobin kinetics.
作者信息
Hargrove M S
机构信息
Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, Iowa 50011, USA.
出版信息
Biophys J. 2000 Nov;79(5):2733-8. doi: 10.1016/S0006-3495(00)76512-X.
Abstract
A flash photolysis method is described for analyzing ligand binding to the new and growing group of hemoglobins which are hexacoordinate in the unligated, ferrous state. Simple analysis of a two exponential fit to time courses for CO rebinding at varying CO concentrations yields rate constants for formation and dissociation of the hexacoordinate complex, and the bimolecular rate constant for CO binding. This method was tested with a nonsymbiotic plant hemoglobin from rice for which these values had not previously been determined. For this protein, dissociation and rebinding of the hexacoordinating amino acid side chain, His(73), is rapid and similar to the rate of CO binding at high CO concentrations. These results indicate that hexacoordination must be taken into account when evaluating the affinity of hexacoordinate hemoglobins for ligands.
摘要
本文描述了一种闪光光解方法，用于分析配体与新出现且不断增加的一类血红蛋白的结合情况，这类血红蛋白在未结合配体的亚铁状态下是六配位的。通过对不同一氧化碳浓度下一氧化碳重新结合的时间进程进行双指数拟合的简单分析，可得出六配位复合物形成和解离的速率常数，以及一氧化碳结合的双分子速率常数。该方法用来自水稻的非共生植物血红蛋白进行了测试，此前尚未测定这些值。对于这种蛋白质，六配位氨基酸侧链His(73)的解离和重新结合很快，且与高一氧化碳浓度下一氧化碳的结合速率相似。这些结果表明，在评估六配位血红蛋白对配体的亲和力时，必须考虑六配位情况。
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