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Biophys J. 1995 Jun;68(6):2497-504. doi: 10.1016/S0006-3495(95)80432-7.
2
Ligand binding to heme proteins: III. FTIR studies of His-E7 and Val-E11 mutants of carbonmonoxymyoglobin.配体与血红素蛋白的结合：III. 一氧化碳肌红蛋白His-E7和Val-E11突变体的傅里叶变换红外光谱研究
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3
Ligand binding to heme proteins: the effect of light on ligand binding in myoglobin.配体与血红素蛋白的结合：光对肌红蛋白中配体结合的影响。
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Ligand binding to heme proteins. VI. Interconversion of taxonomic substates in carbonmonoxymyoglobin.配体与血红素蛋白的结合。VI. 一氧化碳肌红蛋白中分类亚态的相互转化。
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Identification of conformational substates involved in nitric oxide binding to ferric and ferrous myoglobin through difference Fourier transform infrared spectroscopy (FTIR).通过差示傅里叶变换红外光谱（FTIR）鉴定参与一氧化氮与高铁肌红蛋白和亚铁肌红蛋白结合的构象亚态。
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The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin.结构、能量景观、动力学和别构在肌红蛋白酶功能中的作用。
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Biophys J. 1996 Sep;71(3):1563-73. doi: 10.1016/S0006-3495(96)79359-1.

本文引用的文献

1
Light-induced and thermal relaxation in a protein.蛋白质中的光诱导和热弛豫
Phys Rev Lett. 1995 Mar 27;74(13):2607-2610. doi: 10.1103/PhysRevLett.74.2607.
2
Glassy behavior of a protein.蛋白质的玻璃态行为。
Phys Rev Lett. 1989 Apr 17;62(16):1916-1919. doi: 10.1103/PhysRevLett.62.1916.
3
Roles of proximal ligand in heme proteins: replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase.近端配体在血红素蛋白中的作用：通过定点诱变将人肌红蛋白的近端组氨酸替换为半胱氨酸和酪氨酸，作为细胞色素P-450、氯过氧化物酶和过氧化氢酶的模型。
Biochemistry. 1993 Jan 12;32(1):241-52. doi: 10.1021/bi00052a031.
4
Structural relaxation and nonexponential kinetics of CO-binding to horse myoglobin. Multiple flash photolysis experiments.一氧化碳与马肌红蛋白结合的结构弛豫和非指数动力学。多次闪光光解实验。
Biophys J. 1993 Jun;64(6):1833-42. doi: 10.1016/S0006-3495(93)81554-6.
5
Ligand binding to heme proteins: II. Transitions in the heme pocket of myoglobin.配体与血红素蛋白的结合：II. 肌红蛋白血红素口袋中的转变
Biophys J. 1993 Oct;65(4):1496-507. doi: 10.1016/S0006-3495(93)81218-9.
6
Structural heterogeneity of the Fe(2+)-N epsilon (HisF8) bond in various hemoglobin and myoglobin derivatives probed by the Raman-active iron histidine stretching mode.通过拉曼活性铁-组氨酸伸缩模式探测的各种血红蛋白和肌红蛋白衍生物中Fe(2+)-Nε(HisF8)键的结构异质性
Biophys J. 1993 Oct;65(4):1470-85. doi: 10.1016/S0006-3495(93)81216-5.
7
Replacement of the proximal ligand of sperm whale myoglobin with free imidazole in the mutant His-93-->Gly.在突变体His-93→Gly中，用游离咪唑取代抹香鲸肌红蛋白的近端配体。
Biochemistry. 1994 May 31;33(21):6546-54. doi: 10.1021/bi00187a023.
8
Anatomy and dynamics of a ligand-binding pathway in myoglobin: the roles of residues 45, 60, 64, and 68.肌红蛋白中配体结合途径的解剖结构与动力学：45、60、64和68位残基的作用
Biochemistry. 1994 May 10;33(18):5518-25. doi: 10.1021/bi00184a021.
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Conformational relaxation and ligand binding in myoglobin.肌红蛋白中的构象弛豫与配体结合
Biochemistry. 1994 May 3;33(17):5128-45. doi: 10.1021/bi00183a017.
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Investigations of the thermal response of laser-excited biomolecules.激光激发生物分子的热响应研究。
Biophys J. 1994 Feb;66(2 Pt 1):430-6. doi: 10.1016/s0006-3495(94)80793-3.

配体与血红素蛋白的结合。V. 一氧化碳肌红蛋白近端突变体L89I和H97F中的光诱导弛豫。

Ligand binding to heme proteins. V. Light-induced relaxation in proximal mutants L89I and H97F of carbonmonoxymyoglobin.

作者信息

Abadan Y, Chien E Y, Chu K, Eng C D, Nienhaus G U, Sligar S G

机构信息

Department of Physics, University of Illinois at Urbana-Champaign 61801, USA.

出版信息

Biophys J. 1995 Jun;68(6):2497-504. doi: 10.1016/S0006-3495(95)80432-7.

DOI:10.1016/S0006-3495(95)80432-7
PMID:7647252
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1282159/
Abstract

We have studied the proximal mutants L89I and H97F of MbCO with FTIR and temperature-derivative spectroscopy at temperatures between 10 and 160 K. The mutations give rise only to minor alterations of the stretch spectra of the bound and photodissociated CO ligand. The most pronounced difference is a larger population in the A3 substate at approximately 1930 cm-1 in the mutants. The barrier distributions, as determined by temperature-derivative spectroscopy, are very similar to native MbCO after short illumination. Extended illumination leads to substantial increases of the rebinding barriers in native MbCO and the proximal mutants. A larger fraction of light-relaxed states is found in the proximal mutants, implying that the conformational energy landscape has been modified to more easily allow light-induced transitions. These and other spectroscopic data imply that the large changes in the binding properties are brought about by a light-induced conformational relaxation involving the structure at the heme iron. Similarities with spectral hole-burning studies and physical models are discussed.

摘要

我们利用傅里叶变换红外光谱（FTIR）和温度导数光谱，在10至160K的温度范围内研究了肌红蛋白一氧化碳（MbCO）的近端突变体L89I和H97F。这些突变仅导致结合态和光解离态一氧化碳配体的伸缩光谱发生微小变化。最显著的差异是，在突变体中，位于约1930 cm-1处的A3亚态存在更大的布居数。通过温度导数光谱确定的能垒分布，在短时间光照后与天然MbCO非常相似。长时间光照会导致天然MbCO和近端突变体的重新结合能垒大幅增加。在近端突变体中发现了更大比例的光弛豫态，这意味着构象能量景观已被改变，从而更容易实现光诱导跃迁。这些以及其他光谱数据表明，结合特性的巨大变化是由涉及血红素铁结构的光诱导构象弛豫引起的。文中还讨论了与光谱烧孔研究和物理模型的相似性。