期刊
RSC ADVANCES
卷 10, 期 73, 页码 44768-44772出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/d0ra09961a
关键词
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资金
- National Natural Science Foundation of China [21977042]
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.
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