Abstract
The tRNA modification queuosine (Q) was first discovered in the wobble position of His, Tyr, Asp, and Asn anticodons over 40 years ago, yet only recently was the final biosynthetic enzyme responsible for Q‐base maturation identified. Even more perplexing was the apparent dependence on cobalamin (B12) and reducing equivalents. Here, we present structural insight into how epoxyqueuosine reductase uses B12 in a new light to react with nucleic acid molecules and expands the exciting family of B12‐dependent enzymes. CLD is an HHMI investigator, and this work was supported by NIH grant GM72623 awarded to VB.
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