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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase / chemistry*
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Animals
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Apoproteins / chemistry*
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Cobalt / chemistry*
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Crystallography, X-Ray
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Escherichia coli / chemistry
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Escherichia coli / enzymology*
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Histidine / chemistry*
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Horses
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Models, Molecular
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Myoglobin / chemistry*
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Oxidation-Reduction
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Vitamin B 12 / chemistry*
Substances
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Apoproteins
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Myoglobin
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apomyoglobin
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Cobalt
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Histidine
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5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase
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Vitamin B 12