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SSRN 2023年

作者： Long, Shuang-Shuang Li, Yan-Yan Yu, Lu Liu, Ao-Kun Gao, Shu-Qin Tan, Xiangshi Lin, Ying-Wu School of Chemistry and Chemical Engineering University of South China Hengyang421001 China High Magnetic Field Laboratory Chinese Academy of Sciences Anhui Hefei230031 China Key Lab of Protein Structure and Function of Universities in Hunan Province University of South China Hengyang421001 China Department of Chemistry Institute of Biomedical Science Fudan University Shanghai200433 China

The sequence and structure of human cytochrome c (hCyt c) exhibit evolutionary conservations, with only a limited number of naturally occurring mutations in humans. Herein, we investigated the effects of naturally occurring S47F/A mutations on the structure and function of hCyt c. Although the naturally occurring S47F/A mutations did not largely alter the protein structure, the S47F and S47A variants exhibited a small fraction of high-spin species. Kinetic studies showed that the peroxidase activity of the variants was enhanced by ~2.5-fold under neutral pH conditions, as well as for the rate in reaction with H2O2, when compared to those of wild-type hCyt c. In addition, we evaluated the interaction between hCyt c and human neuroglobin (hNgb) by isothermal titration calorimetry (ITC) studies, which revealed that the binding constant was reduced by ~8-fold as result of the mutation of the hydrophilic Ser to the hydrophobic Phe/Ala. These findings provide valuable insights into the role of Ser47 in W-loop C in sustaining the structure and function of hCyt c. © 2023, The Authors. All rights reserved.

关键词： proteins

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