在非天然状态下，将人神经球蛋白工程化为具有单个硫醚键的细胞色素 c 样蛋白。

Engineering Human Neuroglobin into a Cytochrome c-Like Protein with a Single Thioether Bond in Non-native State.

机构信息

School of Chemistry and Chemical Engineering, University of South China, Hengyang, 421001, China.

Department of Chemistry & Institute of Biomedical Science, Fudan University, Shanghai, 200433, China.

出版信息

Chembiochem. 2022 Dec 5;23(23):e202200531. doi: 10.1002/cbic.202200531. Epub 2022 Nov 2.

DOI:10.1002/cbic.202200531

PMID:36217897

Abstract

A double mutant of human H64M/V71C neuroglobin (Ngb) was engineered, which formed a single thioether bond as that in atypical cytochrome c, whereas the heme distal Met64 was oxidized to both sulfoxide (SO-Met) and sulfone (SO -Met). By contrast, no Cys-heme cross-link was formed in V71C Ngb with His64/His96 coordination, as shown by the X-ray crystal structure, which indicates that an open distal site facilitates the activation of heme iron for structural modifications.

摘要

人源 H64M/V71C 神经红蛋白（Ngb）的双突变体被构建，其形成了类似于典型细胞色素 c 的单个硫醚键，而血红素远端的 Met64 则被氧化为亚砜（SO-Met）和砜（SO -Met）。相比之下，在 His64/His96 配位的 V71C Ngb 中，没有形成 Cys-血红素交联，这可以从 X 射线晶体结构中看出，这表明开放的远端位点有利于血红素铁的活化，从而进行结构修饰。