Co(II)/Co(I) reduction-induced axial histidine-flipping in myoglobin reconstituted with a cobalt tetradehydrocorrin as a methionine synthase model

Chem Commun (Camb). 2014 Oct 25;50(83):12560-3. doi: 10.1039/c4cc05448b.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase / chemistry*
  • Animals
  • Apoproteins / chemistry*
  • Cobalt / chemistry*
  • Crystallography, X-Ray
  • Escherichia coli / chemistry
  • Escherichia coli / enzymology*
  • Histidine / chemistry*
  • Horses
  • Models, Molecular
  • Myoglobin / chemistry*
  • Oxidation-Reduction
  • Vitamin B 12 / chemistry*

Substances

  • Apoproteins
  • Myoglobin
  • apomyoglobin
  • Cobalt
  • Histidine
  • 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase
  • Vitamin B 12