Aojula H S, Wilson M T, Morrison I G
Biochem J. 1987 Apr 1;243(1):205-10. doi: 10.1042/bj2430205.
Ligand-binding kinetics of native and reconstituted sperm-whale myoglobin were studied in relation to haem orientational disorder by rapid kinetic methods. In addition, native yellow-fin-tuna myoglobin with significant amount of haem disorder was also used. The O2 dissociation and association rates were found for the proteins with different degrees of haem disorder, and these results suggest that the isomers are characterized by almost identical kinetic parameters. Rates of CO recombination after photolysis were also identical for the two orientational isomers. The results clearly indicate that the rotation of the haem about the alpha-gamma meso axis has little or no effect on the ligand-binding properties of these myoglobins.
通过快速动力学方法研究了天然和重组抹香鲸肌红蛋白的配体结合动力学与血红素取向紊乱的关系。此外,还使用了具有大量血红素紊乱的天然黄鳍金枪鱼肌红蛋白。测定了具有不同程度血红素紊乱的蛋白质的氧气解离和缔合速率,这些结果表明异构体具有几乎相同的动力学参数。两种取向异构体光解后的一氧化碳重组速率也相同。结果清楚地表明,血红素围绕α-γ中轴的旋转对这些肌红蛋白的配体结合特性几乎没有影响。