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高铁血红蛋白的多个血红素口袋亚构象与远端组氨酸相互作用相关。

Multiple heme pocket subconformations of methemoglobin associated with distal histidine interactions.

作者信息

Levy A, Kuppusamy P, Rifkind J M

机构信息

Laboratory of Cellular and Molecular Biology, National Institute on Aging, National Institutes of Health, Baltimore, Maryland 21224.

出版信息

Biochemistry. 1990 Oct 9;29(40):9311-6. doi: 10.1021/bi00492a002.

DOI:10.1021/bi00492a002
PMID:2174256
Abstract

Electron paramagnetic resonance spectra of methemoglobin reveal that, in addition to the major tetragonal high-spin aqueous complex and the low-spin hydroxide complex, three other complexes associated with the interaction of the distal histidine are resolved. These are a rhombic high-spin and two classes of low-spin bis-histidine complexes. By freeze-quenching experiments it is shown that the rhombic high-spin and one of the low-spin bis-histidine complexes (B) are at equilibrium with the dominant species. Incubation in the 210-260 K temperature range shifts the total equilibrium toward a low-energy state with the distal histidine coordinated to the iron (complex C).

摘要

高铁血红蛋白的电子顺磁共振光谱显示,除了主要的四方高自旋水合络合物和低自旋氢氧化物络合物外,还分辨出与远端组氨酸相互作用相关的另外三种络合物。它们是菱形高自旋和两类低自旋双组氨酸络合物。通过冷冻猝灭实验表明,菱形高自旋和一种低自旋双组氨酸络合物(B)与主要物种处于平衡状态。在210 - 260 K温度范围内孵育会使总平衡向低能态移动,此时远端组氨酸与铁配位(络合物C)。

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