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

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 peroxidas...

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Detalles Bibliográficos
Autores principales: Lou, Dan, Liu, Xi-Chun, Wang, Xiao-Juan, Gao, Shu-Qin, Wen, Ge-Bo, Lin, Ying-Wu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2020
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9058552/
https://www.ncbi.nlm.nih.gov/pubmed/35516242
http://dx.doi.org/10.1039/d0ra09961a
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author Lou, Dan
Liu, Xi-Chun
Wang, Xiao-Juan
Gao, Shu-Qin
Wen, Ge-Bo
Lin, Ying-Wu
author_facet Lou, Dan
Liu, Xi-Chun
Wang, Xiao-Juan
Gao, Shu-Qin
Wen, Ge-Bo
Lin, Ying-Wu
author_sort Lou, Dan
collection PubMed
description 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 H(2)O(2). 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.
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spelling pubmed-90585522022-05-04 The importance of Asn52 in the structure–function relationship of human cytochrome c Lou, Dan Liu, Xi-Chun Wang, Xiao-Juan Gao, Shu-Qin Wen, Ge-Bo Lin, Ying-Wu RSC Adv Chemistry 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 H(2)O(2). 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. The Royal Society of Chemistry 2020-12-18 /pmc/articles/PMC9058552/ /pubmed/35516242 http://dx.doi.org/10.1039/d0ra09961a Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/
spellingShingle Chemistry
Lou, Dan
Liu, Xi-Chun
Wang, Xiao-Juan
Gao, Shu-Qin
Wen, Ge-Bo
Lin, Ying-Wu
The importance of Asn52 in the structure–function relationship of human cytochrome c
title The importance of Asn52 in the structure–function relationship of human cytochrome c
title_full The importance of Asn52 in the structure–function relationship of human cytochrome c
title_fullStr The importance of Asn52 in the structure–function relationship of human cytochrome c
title_full_unstemmed The importance of Asn52 in the structure–function relationship of human cytochrome c
title_short The importance of Asn52 in the structure–function relationship of human cytochrome c
title_sort importance of asn52 in the structure–function relationship of human cytochrome c
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9058552/
https://www.ncbi.nlm.nih.gov/pubmed/35516242
http://dx.doi.org/10.1039/d0ra09961a
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