Abstract
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. © 2014 Partner Organisations.
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CITATION STYLE
Hayashi, T., Morita, Y., Mizohata, E., Oohora, K., Ohbayashi, J., Inoue, T., & Hisaeda, Y. (2014). Co(II)/Co(I) reduction-induced axial histidine-flipping in myoglobin reconstituted with a cobalt tetradehydrocorrin as a methionine synthase model. Chemical Communications, 50(83), 12560–12563. https://doi.org/10.1039/c4cc05448b
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