The mechanism of cobalamin binding to hog intrinsic factor

Eric L. Lien; Leon Ellenbogen; P. Y. Law; J. M. Wood

doi:10.1016/0006-291X(73)91205-9

The mechanism of cobalamin binding to hog intrinsic factor

Eric L. Lien, Leon Ellenbogen, P. Y. Law, J. M. Wood

Research output: Contribution to journal › Article › peer-review

14 Scopus citations

Abstract

Circular dichroism studies on the methylcobalamin-intrinsic factor complex, together with studies on the carbethoxylation of histidine residues in this complex, indicate that 5,6 dimethylbenzimidazole is probably displaced by a histidine residue of intrinsic factor which coordinates to the cobalt atom at the sixth coordination site. In addition, the stability of the CoC σ bond for methylcobalamin bound to intrinsic factor is identical to that stability measured for the free methyl-cobinamide-histidine complex, but considerably different from the stability of this σ bond in free methylcobalamin.

Original language	English (US)
Pages (from-to)	730-735
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	55
Issue number	3
DOIs	https://doi.org/10.1016/0006-291X(73)91205-9
State	Published - Dec 10 1973
Externally published	Yes

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AU - Lien, Eric L.

AU - Ellenbogen, Leon

AU - Law, P. Y.

AU - Wood, J. M.

PY - 1973/12/10

Y1 - 1973/12/10

N2 - Circular dichroism studies on the methylcobalamin-intrinsic factor complex, together with studies on the carbethoxylation of histidine residues in this complex, indicate that 5,6 dimethylbenzimidazole is probably displaced by a histidine residue of intrinsic factor which coordinates to the cobalt atom at the sixth coordination site. In addition, the stability of the CoC σ bond for methylcobalamin bound to intrinsic factor is identical to that stability measured for the free methyl-cobinamide-histidine complex, but considerably different from the stability of this σ bond in free methylcobalamin.

AB - Circular dichroism studies on the methylcobalamin-intrinsic factor complex, together with studies on the carbethoxylation of histidine residues in this complex, indicate that 5,6 dimethylbenzimidazole is probably displaced by a histidine residue of intrinsic factor which coordinates to the cobalt atom at the sixth coordination site. In addition, the stability of the CoC σ bond for methylcobalamin bound to intrinsic factor is identical to that stability measured for the free methyl-cobinamide-histidine complex, but considerably different from the stability of this σ bond in free methylcobalamin.

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The mechanism of cobalamin binding to hog intrinsic factor

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