对氧合血红蛋白中O---O和Fe---O2伸缩振动模式的同步观测。
Simultaneous observation of the O---O and Fe---O2 stretching modes in oxyhemoglobins.
作者信息
Das T K, Couture M, Ouellet Y, Guertin M, Rousseau D L
机构信息
Department of Physiology and Biophysics, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
出版信息
Proc Natl Acad Sci U S A. 2001 Jan 16;98(2):479-84. doi: 10.1073/pnas.98.2.479.
Abstract
Understanding of the chemical nature of the dioxygen moiety of oxyhemoglobin is crucial for elucidation of its physiological function. In the present work, direct Raman spectroscopic observation of both the FeO(2) and OO stretching modes unambiguously establishes the vibrational characteristics of the oxygen-bound heme moiety in the hemoglobins of Chlamydomonas eugametos and Synechocystis PCC6803. In addition to providing the resonance Raman assignment of the OO stretching mode (1136 cm(-1) for Chlamydomonas, 1133 cm(-1) for Synechocystis) in an oxyhemoglobin with an iron-porphyrin, this study also reports unusually low frequencies for the FeO(2) stretching modes (554 cm(-1)). The effect of strong hydrogen bonding to the bound oxygen is confirmed by changes in the frequency of the FeO(2) stretching mode on mutation of distal residues. These findings suggest an enzymatic function rather than an oxygen transport role for these hemoglobins.
摘要
了解氧合血红蛋白中二氧部分的化学性质对于阐明其生理功能至关重要。在本研究中，通过直接拉曼光谱观察FeO(2)和OO伸缩模式，明确确定了衣藻和聚球藻PCC6803血红蛋白中氧结合血红素部分的振动特征。除了给出铁卟啉氧合血红蛋白中OO伸缩模式（衣藻为1136 cm(-1)，聚球藻为1133 cm(-1)）的共振拉曼归属外，本研究还报道了FeO(2)伸缩模式的异常低频（554 cm(-1)）。通过远端残基突变时FeO(2)伸缩模式频率的变化，证实了与结合氧的强氢键作用。这些发现表明这些血红蛋白具有酶功能而非氧运输作用。
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