Issue 73, 2020, Issue in Progress
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RSC Advances

The importance of Asn52 in the structure–function relationship of human cytochrome c†

Dan Lou,‡a   Xi-Chun Liu,‡a   Xiao-Juan Wang,a   Shu-Qin Gao,b   Ge-Bo Wenb  and  Ying-Wu Lin ORCID logo *ab  

* Corresponding authors

a School of Chemistry and Chemical Engineering, University of South China, Hengyang 421001, China
E-mail: ywlin@usc.edu.cn

b Laboratory of Protein Structure and Function, University of South China Medical School, Hengyang 421001, China

Abstract

The function of the highly conserved residue Asn52 in human cytochrome c (H-Cyt c) is not fully understood. Herein, we show that the naturally occurring variant N52S H-Cyt c has a perturbed secondary structure, with a small fraction of high-spin species. Remarkably, it exhibits an enhanced peroxidase activity by 3–8-fold at neutral pH, as well as self-oxidation in reaction with H2O2. This study suggests that the H-bond network mediated by Asn52 is essential to suppress the apoptotic activity of H-Cyt c under physiological conditions.

Graphical abstract: The importance of Asn52 in the structure–function relationship of human cytochrome c

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Article information

DOI
https://doi.org/10.1039/D0RA09961A
Article type
Paper
Submitted
24 Nov 2020
Accepted
07 Dec 2020
First published
18 Dec 2020
This article is Open Access
Creative Commons BY-NC license

RSC Adv., 2020,10, 44768-44772

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The importance of Asn52 in the structure–function relationship of human cytochrome c

D. Lou, X. Liu, X. Wang, S. Gao, G. Wen and Y. Lin, RSC Adv., 2020, 10, 44768 DOI: 10.1039/D0RA09961A

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