Methionine synthase: Difference between revisions
No edit summary |
No edit summary |
||
| Line 21: | Line 21: | ||
'''Co(III)alamin''': Cobalt in +3 oxidation state occurs when His 759 replaces the dimethylbenzimidazole (DMB) ligand to allow for the methyl to be accepted by Cob(I)alamin, forming Me-Cob(III)alamin. | '''Co(III)alamin''': Cobalt in +3 oxidation state occurs when His 759 replaces the dimethylbenzimidazole (DMB) ligand to allow for the methyl to be accepted by Cob(I)alamin, forming Me-Cob(III)alamin. | ||
'''Cob(II)alamin''': Cob(I)alamin is highly reactive towards oxygen so occasionally under aerobic conditions, Cob(I)alamin will undergo oxidation leading to an inactive Cob(II)alamin enzyme in the +2 oxidation state. This is regulated by reductive methylation by using Flavodoxin as an electron donor to reactivate Cob(I)alamin, and subsequently regenerates Me-Cob(III)alamin with a methyl being donated from SAM. | '''Cob(II)alamin''': Cob(I)alamin is highly reactive towards oxygen so occasionally under aerobic conditions, Cob(I)alamin will undergo oxidation leading to an inactive Cob(II)alamin enzyme in the +2 oxidation state. This is regulated by reductive methylation by using Flavodoxin as an electron donor to reactivate Cob(I)alamin, and subsequently regenerates Me-Cob(III)alamin with a methyl being donated from SAM<ref>DOI:10.1073/pnas.1133218100</ref>. | ||
=== Relevance === | === Relevance === | ||
| Line 73: | Line 73: | ||
The Cobalamin binding domain has a special characteristic in that, it is most naturally found in a protective conformation to prevent unwanted chemistry from occurring (PDB: 1BMT). This is referred to as a 'capping' mechanism. | The Cobalamin binding domain has a special characteristic in that, it is most naturally found in a protective conformation to prevent unwanted chemistry from occurring (PDB: 1BMT). This is referred to as a 'capping' mechanism. | ||
DMB, in the lower ligand of the <scene name='90/907471/Bindingdomain2/1'>B12 binding domain</scene> is displaced from the Cobalt by a Histidine residue to be 'uncapped' to form Me-Cob(III)alamin. | DMB, in the lower ligand of the <scene name='90/907471/Bindingdomain2/1'>B12 binding domain</scene> is displaced from the Cobalt by a Histidine residue to be 'uncapped' to form Me-Cob(III)alamin<ref>DOI:10.1146/annurev.biochem.72.121801.161828</ref>. | ||
| Line 121: | Line 121: | ||
=== References === | === References === | ||
<references/> | <references/> | ||
[[Category:One-carbon metabolism]] | [[Category:One-carbon metabolism]] | ||