Crystallization (Comment) | Organism |
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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 | UniProt | Comment | Textmining |
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synthetic construct | - |
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Cofactor | Comment | Organism | Structure |
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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 |