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Updated: Sep 24, 2025

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry
Published on: March 13, 2014
The importance of Asn52 in the structure-function relationship of human cytochrome c
Dan Lou1, Xi-Chun Liu1, Xiao-Juan Wang1
1School of Chemistry and Chemical Engineering, University of South China Hengyang 421001 China ywlin@usc.edu.cn.
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.
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