血红素蛋白中血红素紊乱的质子核磁共振表征
Proton nuclear magnetic resonance characterization of heme disorder in hemoproteins.
作者信息
La Mar G N, Budd D L, Viscio D B, Smith K M, Langry K C
出版信息
Proc Natl Acad Sci U S A. 1978 Dec;75(12):5755-9. doi: 10.1073/pnas.75.12.5755.
Abstract
A proton NMR method is described for determining the orientation of a porphyrin within the heme pocket of a hemoprotein. The pattern of the hyperfine-shifted heme methyl resonances in low-spin ferric model compounds is demonstrated to characteristically reflect the position of a localized low-symmetry perturbation on the pi system. The specific assignments via deuteration of the two interconvertible sets of methyl resonances observed for deuteroporphyrin-reconstituted sperm whale metmyoglobin cyanide lead to the conclusion that the low-symmetry perturbations on the heme due to the apo-protein contacts differ for the two protein components by a 180 degrees rotation about the alpha-gamma meso axis. Hence the heme in the reconstituted myoglobin is "disordered" in solution, and the altered functional properties of the reconstituted protein cannot be simply attributed to the local effect of the heme substituent. This NMR technique has applicability for determining the relative heme orientation in related hemoproteins, and may clarify the origin of doubling of heme resonances observed in several native hemoproteins.
摘要
描述了一种用于确定卟啉在血红蛋白血红素口袋内取向的质子核磁共振方法。低自旋铁模型化合物中高精细位移的血红素甲基共振模式被证明可特征性地反映π体系上局部低对称扰动的位置。通过对氘代卟啉重构的抹香鲸高铁肌红蛋白氰化物中观察到的两组可相互转换的甲基共振进行氘代，得出的具体归属表明，由于脱辅基蛋白接触而导致的血红素上的低对称扰动，对于两种蛋白质组分而言，绕α-γ中位轴旋转180度会有所不同。因此，重构肌红蛋白中的血红素在溶液中是“无序的”，重构蛋白功能特性的改变不能简单地归因于血红素取代基的局部效应。这种核磁共振技术适用于确定相关血红蛋白中血红素的相对取向，并可能阐明在几种天然血红蛋白中观察到的血红素共振加倍的起源。
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本文引用的文献
1
STUDIES ON THE STRUCTURE OF HEMOGLOBIN. III. PHYSICOCHEMICAL PROPERTIES OF RECONSTITUTED HEMOGLOBINS.
Biochim Biophys Acta. 1964 Mar 30;79:284-92. doi: 10.1016/0926-6577(64)90009-9.
2
Cleavage of the haem-protein link by acid methylethylketone.酸性甲乙酮对血红素-蛋白质连接的裂解作用。
Biochim Biophys Acta. 1959 Oct;35:543. doi: 10.1016/0006-3002(59)90407-x.
3
Substituted deuteroporphyrins. I. Reactions at the periphery of the porphyrin ring.
J Org Chem. 1966 Aug;31(8):2631-40. doi: 10.1021/jo01346a042.
4
[Formyl-and acetyl-substituted deuteroporphyrines].[甲酰基和乙酰基取代的原卟啉]
Justus Liebigs Ann Chem. 1968;718:148-61. doi: 10.1002/jlac.19687180116.
5
Oxygen equilibrium of hemoglobins containing unnatural hemes. Effect of modification of heme carboxyl groups and side chains at positions 2 and 4.
J Biol Chem. 1971 Jan 25;246(2):389-94.
6
Nuclear magnetic resonances of reconstituted myoglobins.重组肌红蛋白的核磁共振
Proc Natl Acad Sci U S A. 1969 Jul;63(3):623-8. doi: 10.1073/pnas.63.3.623.
7
The atomic structure of erythrocruorin in the light of the chemical sequence and its comparison with myoglobin.基于化学序列的蚯蚓血红蛋白原子结构及其与肌红蛋白的比较。
Eur J Biochem. 1971 Mar 1;19(1):42-50. doi: 10.1111/j.1432-1033.1971.tb01285.x.
8
Three-dimensional structure of hemoglobin from the polychaete annelid, Glycera dibranchiata, at 2.5 A resolution.多毛纲环节动物双鳃裂虫血红蛋白在2.5埃分辨率下的三维结构。
J Biol Chem. 1974 Jul 10;249(13):4067-78.
9
Studies on modified hemoglobins. IV. Hybrid hemoglobins containing proto- and mesohemes and their oxygenation characteristics.
J Biol Chem. 1974 Dec 25;249(24):7964-8.
10
Assignments of the paramagnetically shifted heme methyl nuclear magnetic resonance peaks of cyanometmyoglobin by selective deuteration.
J Mol Biol. 1974 Jul 15;86(4):749-56. doi: 10.1016/0022-2836(74)90351-9.
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