Construction of a highly stable artificial glutathione peroxidase on a protein nanoring

Lu Miao, Xiyu Zhang, Chengye Si, Yuzhou Gao, Linlu Zhao, Chunxi Hou, Oded Shoseyov, Quan Luo*, Junqiu Liu

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

Stable Protein One (SP1) is a boiling-stable oligomeric protein. The unique characteristics of SP1 offer a scaffold to design artificial enzymes against extreme temperature. Here, an efficient antioxidase is successfully constructed on the ring-shaped SP1 homododecamer. By means of computational design and genetic engineering, the active center of glutathione peroxidase (GPx), selenocysteine (Sec), is introduced to the SP1 monomer surface, and the self-assembly properties of the protein monomer lead to a ring-shaped SP1 with homododecamer catalytic selenium centers. This artificial selenoenzyme exhibits high GPx catalytic activity and shows a typical ping-pong kinetic mechanism. Moreover, it has a significantly broader temperature range and high thermostability. Owing to having multi-GPx active centers on a SP1 oligomer, this selenium-containing biomacromolecule exerts an excellent capability to protect cells from oxidative damage at the mitochondrial level. This strategy represents a new way to develop thermostable artificial nanoenzymes for some specific applications.

Original languageAmerican English
Pages (from-to)362-369
Number of pages8
JournalOrganic and Biomolecular Chemistry
Volume12
Issue number2
DOIs
StatePublished - 14 Jan 2014

Fingerprint

Dive into the research topics of 'Construction of a highly stable artificial glutathione peroxidase on a protein nanoring'. Together they form a unique fingerprint.

Cite this