Chinese Journal of Magnetic Resonance >

2023 , Vol. 40 >Issue 3: 246 - 257

DOI: https://doi.org/10.11938/cjmr20222996

Articles

NMR Study on the Mechanism of Cytochrome c Methionine Oxidation

  • Beibei ZHAO ,
  • Jianhua ZHAN ,
  • Qin HU ,
  • Qinjun ZHU ,
  • Maili LIU ,
  • Xu ZHANG
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  • 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 Research Center for Optoelectronics, Huazhong University of Science and Technology, Wuhan 430074, China
    4. Optics Valley Laboratory, Wuhan 430074, China

Received date: 2022-04-10

  Online published: 2022-05-12

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Abstract

Mitochondria generate reactive oxygen species (ROS) during respiration. Low levels of ROS are conducive to signal transduction, whereas excessive accumulation of ROS can lead to protein oxidative modification. Cytochrome c (cyt c) is a multifunctional metalloprotein located in mitochondria. The oxidative modification of cyt c, especially the Met80 has been found to result in conformational change, but the mechanism is still unclear. In this study, the terminal methyl group of methionine on cytochrome c was selectively labeled with 13C, and the modification of the methionine in cytochrome c under oxidative environments was tracked by NMR. It was observed that under oxidative environments, the protein was first converted from reduced state to oxidized state, then oxidatively modified. The oxidative modification of Met80 occurred under relatively high content of ROS, but did not result in distinctive conformation transition. The result suggests that the protein has high activity to resist ROS damage, therefore, plays a regulatory role in inhibiting apoptosis.

Key words： oxidative modification; cytochrome c; liquid-state NMR; selective labeling

Cite this article

Beibei ZHAO , Jianhua ZHAN , Qin HU , Qinjun ZHU , Maili LIU , Xu ZHANG . NMR Study on the Mechanism of Cytochrome c Methionine Oxidation[J]. Chinese Journal of Magnetic Resonance, 2023 , 40(3) : 246 -257 . DOI: 10.11938/cjmr20222996

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