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Themodynamic and Transport Properties of Intermediate States of the Photocyclic Reaction of Photoactive Yellow Protein

机译：光敏黄色蛋白光循环反应中间态的热力学和输运性质

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Themodynamic and transport properties of intermediate state of the photocyclic reaction of photoactive yellow protein (PYP) were studied by a combination of the pulsed laser-induced transient grating (TG), transient lens (TrL), and photoacoustic (PA) spectroscopies from tens of nanoseconds to hundreds of milliseconds. The diffusion coefficients (D) of PYP in the ground state (pG) and of the second intermediate state (pB) were determined by the TG analysis, and it was found that D of pG is about 1.2 times larger than D of pB. At the same time, D at various denatured conditions were measured using guanidine hydrochloride as the denaturant. D of completely unfolded protein is about 0.4 times that of the native form. The enthalpy of pB is estimated to be 60 kJ/mol by the TrL method with an assumption that the volume change of pB is not sensitive to the temperature. Since the enthalpy of the first intermediate state (pR) is as high as 160 kJ/mol, it implies that most of the photon energy is stored as the strain of the protein in pR, and this may be the driving force for the successive reaction to pB. From the temperature dependence of the volume change, the difference in the thermal expansion coefficients between pG and pR was calculated. All of the characteristic features of PYP, the negative volume change, the larger thermal expansion coefficient, and the slower diffusion process, indicate that the intermediate pR and pB are reasonably interpreted in terms of the unfolded (loosened) protein structure.
机译：通过脉冲激光诱导的瞬态光栅（TG），瞬态透镜（TrL）和光声（PA）光谱学的结合，研究了光活化黄色蛋白（PYP）的光环反应中间态的热力学和传输性质。纳秒到几百毫秒。通过TG分析确定基态（pG）和第二中间状态（pB）的PYP的扩散系数（D），并且发现pG的D约为pB的D的1.2倍。同时，使用盐酸胍作为变性剂，测定了各种变性条件下的D。完全展开的蛋白质的D约为天然形式的D的0.4倍。在假定pB的体积变化对温度不敏感的情况下，通过TrL方法估计pB的焓为60 kJ / mol。由于第一中间态（pR）的焓高达160 kJ / mol，这意味着大部分光子能量作为pR中蛋白质的应变存储，这可能是后续反应的驱动力到pB。根据体积变化的温度依赖性，计算出pG和pR之间的热膨胀系数之差。 PYP的所有特征，负体积变化，较大的热膨胀系数和较慢的扩散过程均表明，根据未折叠的（松散的）蛋白质结构合理解释了中间的pR和pB。

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