Journal
RSC ADVANCES
Volume 10, Issue 73, Pages 44768-44772Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d0ra09961a
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Funding
- National Natural Science Foundation of China [21977042]
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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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