Cytochrome c injection induced embryo loss

Xu, Tonghui; Yang, Qiuhong; Wang, Banqin; Wang, Wenfu; Li, Jingxin; Ma, Yuyan; Gao, Xiaolin

doi:10.1080/01480545.2019.1643873

Cited by 1 publication

(2 citation statements)

References 16 publications

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“…1,2 It also acts as a scavenger to resist oxidation damage, 3 making it a useful first-aid medicine for hypoxia. 4 In addition, cyt c induces cell apoptosis when released to the cytosol under certain stimuli, such as DNA damage or oxidative stress. 5,6 To meet multifunctional needs, the conformation of cyt c shows flexibility and high adaptability.…”

Section: ■ Introductionmentioning

confidence: 99%

“…Cytochrome c (cyt c) is a highly conserved heme protein that transfers electrons in the respiration chain of mitochondria. , It also acts as a scavenger to resist oxidation damage, making it a useful first-aid medicine for hypoxia . In addition, cyt c induces cell apoptosis when released to the cytosol under certain stimuli, such as DNA damage or oxidative stress. , …”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Real-Time Observation of Conformational Changes and Translocation of Endogenous Cytochrome c within Intact Mitochondria

Zhan,

Zeng,

Xiao

et al. 2024

J. Am. Chem. Soc.

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Cytochrome c (cyt c) is a multifunctional protein with varying conformations. However, the conformation of cyt c in its native environment, mitochondria, is still unclear. Here, we applied NMR spectroscopy to investigate the conformation and location of endogenous cyt c within intact mitochondria at natural isotopic abundance, mainly using widespread methyl groups as probes. By monitoring time-dependent chemical shift perturbations, we observed that most cyt c is located in the inner mitochondrial membrane and partially unfolded, which is distinct from its native conformation in solution. When suffering oxidative stress, cyt c underwent oxidative modifications due to increasing reactive oxygen species (ROS), weakening electrostatic interactions with the membrane, and gradually translocating into the inner membrane spaces of mitochondria. Meanwhile, the lethality of oxidatively modified cyt c to cells was reduced compared with normal cyt c. Our findings significantly improve the understanding of the molecular mechanisms underlying the regulation of ROS by cyt c in mitochondria. Moreover, it highlights the potential of NMR to monitor high-concentration molecules at a natural isotopic abundance within intact cells or organelles.

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