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Literature summary for 2.1.1.13 extracted from

  • Hayashi, T.; Morita, Y.; Mizohata, E.; Oohora, K.; Ohbayashi, J.; Inoue, T.; Hisaeda, Y.
    Co(II)/Co(I) reduction-induced axial histidine-flipping in myoglobin reconstituted with a cobalt tetradehydrocorrin as a methionine synthase model (2014), Chem. Commun. (Camb. ), 50, 12560-12563.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
design and preparation of myoglobin reconstituted with the cobalt corrinoid complex, Co(TDHC) as a simple model for the active site. In the heme pocket of myoglobin, CoII(TDHC) is tightly bound and provides a model of the baseoff/His-on state of the cobalamin binding domain of methionine synthase, and the intermediate, the tetra-coordinated Co(I) species, is detectable in the protein matrix synthetic construct

Organism

Organism UniProt Comment Textmining
synthetic construct
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Cofactor

Cofactor Comment Organism Structure
Cobalamin preparation of a synthetic conjugate between apomyoglobin and cobalt tetradehydrocorrin to replicate the coordination behavior of cob(I)alamin in methionine synthase. The tetracoordinated 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 synthetic construct