3wft | pdb_00003wft
From Proteopedia
Crystal structure of horse heart myoglobin reconstituted with cobalt(II) tetradehydrocorrin
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Structural highlights
Publication Abstract from PubMedA 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. Co(II)/Co(I) reduction-induced axial histidine-flipping in myoglobin reconstituted with a cobalt tetradehydrocorrin as a methionine synthase model.,Hayashi T, Morita Y, Mizohata E, Oohora K, Ohbayashi J, Inoue T, Hisaeda Y Chem Commun (Camb). 2014 Oct 25;50(83):12560-3. doi: 10.1039/c4cc05448b. PMID:25197974[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 09:32, 3 December 2014.