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Crystal structure of horse heart myoglobin reconstituted with cobalt(II) tetradehydrocorrinCrystal structure of horse heart myoglobin reconstituted with cobalt(II) tetradehydrocorrin
Structural highlights
Function[MYG_HORSE] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. 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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