Thiol-disulfide redox dependence of heme binding and heme ligand switching in nuclear hormone receptor rev-erb{beta}.

@article{Gupta2011ThioldisulfideRD,
  title={Thiol-disulfide redox dependence of heme binding and heme ligand switching in nuclear hormone receptor rev-erb\{beta\}.},
  author={Nirupama Gupta and Stephen W Ragsdale},
  journal={The Journal of biological chemistry},
  year={2011},
  volume={286 6},
  pages={4392-403}
}
Rev-erbβ is a heme-binding nuclear hormone receptor that represses a broad spectrum of target genes involved in regulating metabolism, the circadian cycle, and proinflammatory responses. Here, we demonstrate that a thiol-disulfide redox switch controls the interaction between heme and the ligand-binding domain of Rev-erbβ. The reduced dithiol state of Rev-erbβ binds heme 5-fold more tightly than the oxidized disulfide state. By means of site-directed mutagenesis and by UV-visible and EPR… CONTINUE READING

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