通过从头设计的二硫键调节结构和功能：肌红蛋白中血红素蛋白的案例研究。
Regulation of both the structure and function by a de novo designed disulfide bond: a case study of heme proteins in myoglobin.
机构信息
School of Chemistry and Chemical Engineering, University of South China, Hengyang 421001, China.
出版信息
Chem Commun (Camb). 2018 Apr 24;54(34):4356-4359. doi: 10.1039/c8cc01646a.
PMID:29645029
Abstract
A de novo designed intramolecular disulfide bond in myoglobin, resembling that in cytoglobin without structural evidence, was confirmed by an X-ray structure for the first time and was demonstrated to regulate both the structure and function of this protein, which fulfills the design of an artificial dehaloperoxidase, with an activity exceeding that of a native enzyme.
摘要
肌红蛋白中首次通过 X 射线结构证实了一种新设计的分子内二硫键，类似于细胞色素 c 中的二硫键，但没有结构证据，该二硫键被证明可以调节该蛋白质的结构和功能，从而实现了人工脱卤过氧化物酶的设计，其活性超过了天然酶。
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