School of Chemistry and Chemical Engineering, University of South China, Hengyang 421001, China; Key Lab of Protein Structure and Function of Universities in Hunan Province, University of South China, Hengyang 421001, China.
J Inorg Biochem. 2024 Aug;257:112595. doi: 10.1016/j.jinorgbio.2024.112595. Epub 2024 May 6.
Globins, such as myoglobin (Mb) and neuroglobin (Ngb), are ideal protein scaffolds for the design of functional metalloenzymes. To date, numerous approaches have been developed for enzyme design. This review presents a summary of the progress made in the design of functional metalloenzymes based on Mb and Ngb, with a focus on the exploitation of covalent interactions, including coordination bonds and covalent modifications. These include the construction of a metal-binding site, the incorporation of a non-native metal cofactor, the formation of Cys/Tyr-heme covalent links, and the design of disulfide bonds, as well as other Cys-covalent modifications. As exemplified by recent studies from our group and others, the designed metalloenzymes have potential applications in biocatalysis and bioconversions. Furthermore, we discuss the current trends in the design of functional metalloenzymes and highlight the importance of covalent interactions in the design of functional metalloenzymes.
球蛋白，如肌红蛋白（Mb）和神经球蛋白（Ngb），是设计功能金属酶的理想蛋白质支架。迄今为止，已经开发出了许多用于酶设计的方法。本综述总结了基于 Mb 和 Ngb 的功能金属酶设计的进展，重点介绍了对共价相互作用的利用，包括配位键和共价修饰。这些方法包括金属结合位点的构建、非天然金属辅因子的掺入、Cys/Tyr-血红素共价键的形成以及二硫键和其他 Cys 共价修饰的设计。正如我们小组和其他小组的最新研究所示，设计的金属酶在生物催化和生物转化中有潜在的应用。此外，我们还讨论了功能金属酶设计的当前趋势，并强调了共价相互作用在功能金属酶设计中的重要性。
