Chinese Journal of Magnetic Resonance (Mar 2023)

Track the Conformational Change of Unlabeled Yeast Cytochrome c in Cell Homogenate Using NMR

  • ZHAN Jianhua,
  • 1. State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan (Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences), Wuhan 430071, China 2. University of Chinese Academy of Sciences, Beijing 100049, China,
  • ZHU Qinjun,
  • JIANG Bin,
  • 1. State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan (Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences), Wuhan 430071, China 2. University of Chinese Academy of Sciences, Beijing 100049, China 3. Wuhan National Laboratory for Optoelectronics, Huazhong University of Science and Technology, Wuhan 430074, China 4. Optics Valley Laboratory, Wuhan 430074, China,
  • LIU Maili

DOI
https://doi.org/10.11938/cjmr20222985
Journal volume & issue
Vol. 40, no. 1
pp. 22 – 29

Abstract

Read online

Cytochrome c (cyt c) is an important multifunctional protein. In mitochondria, it acts as a carrier for electron transporting. In cytoplasm, it may act as an apoptotic initiator to initiate the apoptotic process. Whether and how a complex cytoplasmic environment affects its conformation has not been confirmed yet. In this study, the conformational changes of wild type saccharomyces cerevisiae iso-1 cyt c in yeast cell homogenate were tracked by methyl-based nuclear magnetic resonance (NMR) technique. At least four different oxidative conformations and one reduced conformation of cyt c were identified in cell homogenate. And over time, the transitions among different conformations of cyt c were observed. The results indicate that the conformation of cyt c changes with environment, which may be closely related to resistance to oxidative stress.

Keywords