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1
The elastomeric rack in biology.生物学中的弹性支架。
Proc Natl Acad Sci U S A. 1971 Oct;68(10):2341-4. doi: 10.1073/pnas.68.10.2341.
2
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3
Hydration change during the aging of phosphorylated human butyrylcholinesterase: importance of residues aspartate-70 and glutamate-197 in the water network as probed by hydrostatic and osmotic pressures.磷酸化人丁酰胆碱酯酶老化过程中的水合变化:通过静水压力和渗透压探测水网络中天冬氨酸-70和谷氨酸-197残基的重要性。
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4
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Protein hydration changes during catalysis: a new mechanism of enzymic rate-enhancement and ion activation/inhibition of catalysis.催化过程中的蛋白质水合变化:酶促反应速率提高及离子激活/抑制催化作用的新机制
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[Contribution of protein conformation to stereochemistry and reactivity of the active center of heme proteins and enzymes. The existence of horseradish peroxidase conformations and their possible role in the catalysis mechanism].[蛋白质构象对血红素蛋白和酶活性中心的立体化学及反应性的贡献。辣根过氧化物酶构象的存在及其在催化机制中的可能作用]
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本文引用的文献

1
THE ACCELERATION OF SPORE DISINFECTION BY URETHAN AND ITS RETARDATION BY HYDROSTATIC PRESSURE.氨基甲酸乙酯对孢子消毒的加速作用及其受静水压的抑制作用
J Bacteriol. 1949 Mar;57(3):359-62. doi: 10.1128/jb.57.3.359-362.1949.
2
THE INFLUENCE OF HYDROSTATIC PRESSURE ON THE GROWTH AND VIABILITY OF TERRESTRIAL AND MARINE BACTERIA.静水压力对陆生和海洋细菌生长及生存能力的影响
J Bacteriol. 1949 Feb;57(2):179-89. doi: 10.1128/jb.57.2.179-189.1949.
3
Hydrostatic pressure reversal of narcosis in tadpoles.蝌蚪麻醉的流体静压逆转
Science. 1950 Jul 21;112(2899):91-2. doi: 10.1126/science.112.2899.91-a.
4
Influence of urethane and of hydrostatic pressure on the growth of bacteriophages T2, T5, T6, and T7.氨基甲酸乙酯和静水压力对噬菌体T2、T5、T6和T7生长的影响。
J Gen Physiol. 1951 May;34(5):529-50. doi: 10.1085/jgp.34.5.529.
5
ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.关于别构转变的本质:一个合理的模型。
J Mol Biol. 1965 May;12:88-118. doi: 10.1016/s0022-2836(65)80285-6.
6
FREE ENERGY CHANGES IN REACTIONS OF CHYMOTRYPSIN WITH SUBSTRATES.胰凝乳蛋白酶与底物反应中的自由能变化
J Biol Chem. 1964 Dec;239:4145-50.
7
MECHANISM OF ENZYME CATALYSIS.酶催化的机制
Nature. 1964 Oct 24;204:342-3. doi: 10.1038/204342a0.
8
Allosteric proteins and cellular control systems.别构蛋白与细胞控制系统。
J Mol Biol. 1963 Apr;6:306-29. doi: 10.1016/s0022-2836(63)80091-1.
9
Reversible denaturation in the myosin adenosine triphosphatase system.肌球蛋白三磷酸腺苷酶系统中的可逆变性
J Cell Comp Physiol. 1958 Aug;52(1):79-87. doi: 10.1002/jcp.1030520106.
10
The pressure, temperature and ion relations of myosin ATP-ase.
J Cell Comp Physiol. 1958 Aug;52(1):59-77. doi: 10.1002/jcp.1030520105.

生物学中的弹性支架。

The elastomeric rack in biology.

作者信息

Eyring H, Johnson F H

出版信息

Proc Natl Acad Sci U S A. 1971 Oct;68(10):2341-4. doi: 10.1073/pnas.68.10.2341.

DOI:10.1073/pnas.68.10.2341
PMID:5289868
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC389417/
Abstract

A model designated "The elastomeric rack" is discussed with reference to the mechanism of enzyme catalysis and the necessity of large protein molecules in the process. This model, which represents an extension of the earlier "Rack mechanism," stems from experimental evidence demonstrating large volume changes of activation or of reaction accompanying various biochemical reactions and more complicated physiological processes. For reasons discussed, the volume changes, as revealed through the influence of increased hydrostatic pressure on reaction rates and equilibria, prove that there are large conformational changes in the protein which, because of numerous cross links in a complex network, lead to additive stress on the substrate-enzyme complex, and thereby to increased reactivity. The manner in which the model serves to account for the influence of changes in the environment (temperature, pressure, chemical composition, electrical fields) on the activity of the protein catalyst, and the modifying action of particular inhibitory or activating substances, alone or in combination, is briefly discussed. The bearing of various considerations on protein denaturation, excitation of nerve, contraction of muscle, specific precipitation, and the divers physiological processes in living cells, including mutation, cancer, and the degenerative diseases of aging, is also briefly discussed.

摘要

文中讨论了一种名为“弹性体支架”的模型,该模型涉及酶催化机制以及该过程中大型蛋白质分子的必要性。此模型是早期“支架机制”的扩展,源于实验证据,这些证据表明,伴随各种生化反应和更复杂的生理过程,活化或反应过程中存在大量体积变化。基于所讨论的原因,通过静水压力增加对反应速率和平衡的影响所揭示的体积变化,证明蛋白质中存在大量构象变化,由于复杂网络中的大量交联,这些变化会对底物 - 酶复合物产生累加应力,从而提高反应活性。文中简要讨论了该模型解释环境变化(温度、压力、化学成分、电场)对蛋白质催化剂活性的影响,以及特定抑制或激活物质单独或组合的修饰作用的方式。还简要讨论了各种因素对蛋白质变性、神经兴奋、肌肉收缩、特异性沉淀以及活细胞中各种生理过程(包括突变、癌症和衰老退行性疾病)的影响。