氧合肌红蛋白和羧基肌红蛋白激发态弛豫和解离的机制。
Mechanisms for excited state relaxation and dissociation of oxymyoglobin and carboxymyoglobin.
作者信息
Reynolds A H, Rand S D, Rentzepis P M
出版信息
Proc Natl Acad Sci U S A. 1981 Apr;78(4):2292-6. doi: 10.1073/pnas.78.4.2292.
Abstract
The dissociation of carboxymyoglobin (MbCO) and oxymyoglobin (MbO2) induced by 530-nm picosecond excitation in the beta band or the 355-nm delta band has been measured by monitoring the absorbance changes at 420 and 440 nm corresponding to ligand-bound and ligand-detached species, respectively. We find that MbO2 and MbCO dissociate with very similar rates, which do not reflect the 30-fold difference between the quantum yields of the two reactions. Kinetic data suggest that a short-lived intermediate is formed that is responsible for the low quantum efficiency of the MbO2 dissociation.
摘要
通过监测分别对应于配体结合态和配体解离态的420和440 nm处的吸光度变化，测量了在β波段530 nm皮秒激发或δ波段355 nm激发下羧基肌红蛋白（MbCO）和氧合肌红蛋白（MbO₂）的解离情况。我们发现，MbO₂和MbCO的解离速率非常相似，这与两个反应的量子产率之间30倍的差异不符。动力学数据表明，形成了一种短寿命中间体，它导致了MbO₂解离的低量子效率。
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