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α-和β-亚硝酰血红蛋白单体光解离的皮秒吸收研究。

Picosecond absorption studies on the photodissociation of alpha- and beta-nitrosyl hemoglobin monomers.

作者信息

Guest C R, Noe L J

机构信息

Department of Chemistry, University of Wyoming, Laramie 82071.

出版信息

Biophys J. 1988 Oct;54(4):731-6. doi: 10.1016/S0006-3495(88)83008-X.

DOI:10.1016/S0006-3495(88)83008-X
PMID:3224153
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1330377/
Abstract

Transient absorption studies of the pump-probe type were performed on the NO forms of the alpha- and beta-monomers of hemoglobin using a Nd3+ phosphate-glass laser. A second harmonic 531-nm, 8-ps fwhm pulse pumped the Q-band while a delayed continuum generated pulse was used to monitor pi pi* Soret absorption changes in the 410-453-nm region. Photodissociation of nitrosyl alpha- and beta-monomers was found to differ markedly from the tetramer in what we believe to be the formation of a five-coordinate HbNO (with proximal imidazole detached) photoproduct within the first 50 ps after photon absorption.

摘要

使用钕掺杂磷酸盐玻璃激光器对血红蛋白α-和β-单体的NO形式进行了泵浦-探测型瞬态吸收研究。一个二次谐波531纳米、半高宽8皮秒的脉冲泵浦Q带，同时使用延迟的连续谱产生脉冲来监测410 - 453纳米区域内ππ*索雷特吸收的变化。我们发现，亚硝酰基α-和β-单体的光解离与四聚体明显不同，我们认为在光子吸收后的前50皮秒内形成了一种五配位的HbNO（近端咪唑脱离）光产物。

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Picosecond absorption studies on the photodissociation of alpha- and beta-nitrosyl hemoglobin monomers.α-和β-亚硝酰血红蛋白单体光解离的皮秒吸收研究。
Biophys J. 1988 Oct;54(4):731-6. doi: 10.1016/S0006-3495(88)83008-X.
2
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本文引用的文献

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Resonance Raman evidence for cleavage of the Fe-N epsilon(His-F8) bond in the alpha subunit of the T-structure nitrosylhemoglobin.共振拉曼光谱证据表明，T结构亚硝基血红蛋白α亚基中Fe-Nε（组氨酸-F8）键发生断裂。
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