Co(II)/Co(I) reduction-induced axial histidine-flipping in myoglobin reconstituted with a cobalt tetradehydrocorrin as a methionine synthase model.

@article{Hayashi2014CoIICoIRA,
  title={Co(II)/Co(I) reduction-induced axial histidine-flipping in myoglobin reconstituted with a cobalt tetradehydrocorrin as a methionine synthase model.},
  author={Takashi Hayashi and Yoshitsugu Morita and Eiichi Mizohata and Koji Oohora and Jun Ohbayashi and Tsuyoshi Inoue and Yoshiio Hisaeda},
  journal={Chemical communications},
  year={2014},
  volume={50 83},
  pages={12560-3}
}
A conjugate between apomyoglobin and cobalt tetradehydrocorrin was prepared to replicate the coordination behavior of cob(I)alamin in methionine synthase. X-ray crystallography reveals that the tetra-coordinated Co(I) species is formed through the cleavage of the axial Co-His93 ligation after the reduction of the penta-coordinated Co(II) cofactor in the heme pocket. 

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