3WFU

Crystal structure of horse heart myoglobin reconstituted with cobalt(I) tetradehydrocorrin

Summary for 3WFU

• Entry DOI: 10.2210/pdb3wfu/pdb
• Related: 3WFT
• Descriptor: Myoglobin, (1R,19R) cobalt tetradehydrocorrin, (1S,19S) cobalt tetradehydrocorrin, ... (5 entities in total)
• Functional Keywords: globin fold, oxygen transport, muscles
• Biological source: Equus caballus (domestic horse,equine)
• Total number of polymer chains: 1
• Total formula weight: 18400.85

Authors

Mizohata, E.,Morita, Y.,Oohora, K.,Hirata, K.,Ohbayashi, J.,Inoue, T.,Hisaeda, Y.,Hayashi, T. (deposition date: 2013-07-23, release date: 2014-12-03, Last modification date: 2024-03-20)

Primary citation

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.
Chem.Commun.(Camb.), 50:12560-12563, 2014

PubMed 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.

PubMed: 25197974
DOI: 10.1039/c4cc05448b

Experimental method

X-RAY DIFFRACTION (1.35 Å)