Borucki Berthold, Joshi Chandra P, Otto Harald, Cusanovich Michael A, Heyn Maarten P
Biophysics Group, Department of Physics, Freie Universität Berlin, 14195 Berlin, Germany.
Biophys J. 2006 Oct 15;91(8):2991-3001. doi: 10.1529/biophysj.106.086645. Epub 2006 Jul 7.
The signaling state of the photoreceptor photoactive yellow protein is the long-lived intermediate I(2)'. The pH dependence of the equilibrium between the transient photocycle intermediates I(2) and I(2)' was investigated. The formation of I(2)' from I(2) is accompanied by a major conformational change. The kinetics and intermediates of the photocycle and of the photoreversal were measured by transient absorption spectroscopy from pH 4.6 to 8.4. Singular value decomposition (SVD) analysis of the data at pH 7 showed the presence of three spectrally distinguishable species: I(1), I(2), and I(2)'. Their spectra were determined using the extrapolated difference method. I(2) and I(2)' have electronic absorption spectra, with maxima at 370 +/- 5 and 350 +/- 5 nm, respectively. Formation of the signaling state is thus associated with a change in the environment of the protonated chromophore. The time courses of the I(1), I(2), and I(2)' intermediates were determined from the wavelength-dependent transient absorbance changes at each pH, assuming that their spectra are pH-independent. After the formation of I(2)' ( approximately 2 ms), these three intermediates are in equilibrium and decay together to the initial dark state. The equilibrium between I(2) and I(2)' is pH dependent with a pK(a) of 6.4 and with I(2)' the main species above this pK(a). Measurements of the pH dependence of the photoreversal kinetics with a second flash of 355 nm at a delay of 20 ms confirm this pK(a) value. I(2) and I(2)' are photoreversed with reversal times of approximately 55 micros and several hundred microseconds, respectively. The corresponding signal amplitudes are pH dependent with a pK(a) of approximately 6.1. Photoreversal from I(2)' dominates above the pK(a). The transient accumulation of I(2)', the active state of photoactive yellow protein, is thus controlled by the proton concentration. The rate constant k(3) for the recovery to the initial dark state also has a pK(a) of approximately 6.3. This equality of the equilibrium and kinetic pK(a) values is not accidental and suggests that k(3) is proportional to [I(2)'].
光感受器光敏黄色蛋白的信号状态是长寿命中间体I(2)'。研究了瞬态光循环中间体I(2)和I(2)'之间平衡的pH依赖性。从I(2)形成I(2)'伴随着主要的构象变化。通过从pH 4.6至8.4的瞬态吸收光谱法测量光循环和光逆转的动力学及中间体。在pH 7下对数据进行奇异值分解(SVD)分析表明存在三种光谱可区分的物种:I(1)、I(2)和I(2)'。使用外推差分法确定了它们的光谱。I(2)和I(2)'具有电子吸收光谱,其最大值分别在370±5和350±5 nm处。因此,信号状态的形成与质子化发色团环境的变化相关。假设I(1)、I(2)和I(2)'中间体的光谱与pH无关,根据每个pH下波长依赖性瞬态吸光度变化确定了它们的时间进程。在I(2)'形成后(约2毫秒),这三种中间体处于平衡状态并一起衰减至初始暗态。I(2)和I(2)'之间的平衡取决于pH,pK(a)为6.4,在该pK(a)以上I(2)'是主要物种。在20毫秒延迟时用355 nm的第二次闪光测量光逆转动力学的pH依赖性证实了该pK(a)值。I(2)和I(2)'的光逆转时间分别约为55微秒和几百微秒。相应的信号幅度取决于pH,pK(a)约为6.1。在pK(a)以上,从I(2)'的光逆转占主导。因此,光敏黄色蛋白活性状态I(2)'的瞬态积累受质子浓度控制。恢复到初始暗态的速率常数k(3)也具有约6.3的pK(a)。平衡和动力学pK(a)值的这种相等并非偶然,表明k(3)与[I(2)']成正比。