Issue 2, 2014

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

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.

Graphical abstract: Construction of a highly stable artificial glutathione peroxidase on a protein nanoring

Supplementary files

Article information

Article type
Paper
Submitted
30 Jul 2013
Accepted
10 Oct 2013
First published
11 Oct 2013

Org. Biomol. Chem., 2014,12, 362-369

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

L. Miao, X. Zhang, C. Si, Y. Gao, L. Zhao, C. Hou, O. Shoseyov, Q. Luo and J. Liu, Org. Biomol. Chem., 2014, 12, 362 DOI: 10.1039/C3OB41561A

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