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MIT biologists solve vitamin puzzle

in a reaction by temporarily holding electrons and then giving them away. Such cofactors are not consumed in the reaction.

Cannibalization of a cofactor has very rarely been observed before in vitamin synthesis or any type of biosynthetic pathway, says Michiko Taga, an MIT postdoctoral fellow in Walker's lab and lead co-author of the Nature paper.

"There are almost no other examples where the cofactor is used as a substrate," she said.

One early clue to BluB's function was that a gene related to it is located near several other genes involved in B12 synthesis in a different bacterium. Still, the researchers were not convinced that one enzyme could perform all of the complicated chemistry needed to produce DMB.

"It looked like a number of things had to happen in order to make the DMB," said Walker. "We originally thought that BluB might be just one of several enzymes involved in DMB synthesis."

Therefore, it came as a surprise when Taga isolated the BluB protein and showed that it could make DMB all by itself.

Nicholas Larsen, lead co-author and a former college classmate of Taga's now at Harvard Medical School, did a crystallographic analysis of the protein after Taga told him about her research over coffee one day. The protein structure he developed clearly shows the "pocket" of BluB where the DMB synthesis reaction takes place.

Still to be explored is the question of why soil bacteria synthesize B12 at all, Walker said. Soil microorganisms don't require B12 to survive, and the plants they attach themselves to don't need it either, so he speculates that synthesizing B12 may enable the bacteria to withstand "challenges" made by the plants during the formation of the symbiotic relationship.

More than 30 genes are involved in vitamin B12 synthesis, and "that's a lot to carry around if you don't need to make it," Walker said.

The full implications of the new research will probably
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Source:Massachusetts Institute of Technology


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