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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >The role of conformational energetic disorder in the catalytic activity of immobilized enzymes
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The role of conformational energetic disorder in the catalytic activity of immobilized enzymes

机译：构象性高能障碍在固定化酶催化活性中的作用

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摘要

We analyze cooperative behavior in a system of immobilized enzymes which incorporates the notion of heterogeneity or disorder in the interactions. In addition to equilibrium phase changes, this system exhibits vitrification or glass-like transitions in which the overall catalytic activity freezes into one of many possible states. It is shown that these long-lived metastable phases can be produced by a combination of disorder, systematic surface and intermolecular interactions, and chemical association effects such as ligand binding. Biophysical consequences of this frozen state include greatly diminished sensitivity of enzymatic activity to thermal and chemical perturbations. This effect coincides with the appearance of a multitude of possible macroscopic catalytic states rather than a single equilibrium state. Our analysis also suggests that high surface coverages will tend to be catalytically inactive if they are fully equilibrated; rather, high activity with high surface coverage is more likely to be associated with vitrified states of surface immobilization and deep or abrupt chemical quenches.
机译：我们分析固定化酶系统中的协同行为，该系统在相互作用中纳入了异质性或无序性的概念。除了平衡相变外，该系统还表现出玻璃化或玻璃状转变，其中总催化活性冻结成许多可能状态之一。结果表明，这些长寿命的亚稳相可以由无序，系统性表面和分子间相互作用以及化学缔合效应（如配体结合）共同产生。这种冷冻状态的生物物理后果包括酶活性对热和化学扰动的敏感性大大降低。该效果与多种可能的宏观催化状态而不是单个平衡状态的出现相吻合。我们的分析还表明，如果完全平衡，高表面覆盖率将趋于无催化活性。相反，具有高表面覆盖率的高活性更可能与表面固定化的玻璃化状态以及深或突然的化学淬灭有关。

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