Picosecond study of the near infrared absorption band of hemoglobin after photolysis of carbonmonoxyhemoglobin.

Picosecond study of the near infrared absorption band of hemoglobin after photolysis of carbonmonoxyhemoglobin.
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碳单氧血红蛋白光解后血红蛋白近红外吸收带的皮秒研究。

DOI:
10.1016/s0006-3495(91)82122-1
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发表时间:
1991
影响因子:
3.4
通讯作者:
Simon,JD
Simon,JD
中科院分区:
生物学3区
文献类型:
--
作者:
Dunn,RC;Simon,JD

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皮秒吸收光谱用于检查 CO 从碳单氧血红蛋白光解离后,血红蛋白近红外吸收带的位置和带形状随时间的变化。对于探测的最早延迟时间 35 ps,瞬态光谱的峰值位于 765 nm,与平衡脱氧血红蛋白的特征红移 6 nm。对于高达 60 ns 的时间延迟,未观察到峰位置或带形状的变化。此外,光谱的位置和形状与光解能量无关,光解能量范围为 15 微焦/脉冲至 150 微焦/脉冲,跨越光子/血红素比率从 0.01 至 2.0 变化的条件。这表明血红素基团的几何形状不松弛,并且周围蛋白质结构的平衡发生在超过 60 ns 的时间尺度上。
Picosecond absorption spectroscopy is used to examine the position and band shape of the near infrared absorption band of hemoglobin as a function of time after the photodissociation of CO from carbonmonoxyhemoglobin. For the earliest delay time probed, 35 ps, the peak of the transient spectrum is at 765 nm, red shifted by 6 nm from that characteristic of equilibrium deoxyhemoglobin. No evolution in either the peak position or band shape is observed for time delays up to 60 ns. In addition, the position and shape of the spectrum are independent of photolysis energies ranging from 15 microJ/pulse to 150 microJ/pulse, spanning conditions under which the photon/heme ratio is varied from 0.01 to 2.0. This indicates that the geometry in the heme group is unrelaxed and that equilibration of the surrounding protein structure occurs on a time scale longer than 60 ns.
DOI: 10.1016/0005-2795(74)90161-5
发表时间: 1974-01-01
期刊: BIOCHIMICA ET BIOPHYSICA ACTA
影响因子: --
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发表时间: 1981
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