金属酶机制与其周转率和金属稳定性有关

Caio B. Castro, Millena P. Ferreira, Caterina G.C. Marques Netto
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引用次数: 6

摘要

金属酶参与多种不同的反应,金属可以表现出不同的作用,如氧化还原化学或底物活化。活化机理主要描述为与金属中心配位后的键极化。然而,对外球机制的忽视会对反应的机理命题产生深远的影响。在外球面配位中,金属以水合形式充当静电活化剂。由于水合作用在这一机制中起着至关重要的作用,金属的稳定性与酶机制的提出有关。在这篇综述中,我们将从EC 1-6中证明金属不稳定性对金属酶机制设计的影响,并将一些酶与其仿生化合物联系起来。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Metalloenzyme mechanisms correlated to their turnover number and metal lability

Metalloenzymes are involved in several different reactions and the metal can display distinct roles, such as redox chemistry or substrate activation. The activation mechanism is mainly described to occur by bond polarization upon coordination to the metal center. However, the disregard of the outer sphere mechanism can have a profound impact on the mechanism proposition of reactions. In the outer sphere coordination, the metal acts as an electrostatic activator in its hydrated form. Since hydration is crucial in this mechanism, metal lability is related to the proposition of an enzyme mechanism. In this review, we will evidence the impact of metal lability in the design of metalloenzyme mechanisms from EC 1–6, correlating some of the enzymes to their biomimetic compounds.

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Current research in chemical biology
Current research in chemical biology Biochemistry, Genetics and Molecular Biology (General)
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