Abstract
Allostery Enzymes often form dimers or higher-order oligomers, even when each active site is isolated and the reactions are simple. But the effect of a neighbor can be profound. Mehrabi et al. used a photolabile compound to initiate a reaction in the enzyme fluoroacetate dehalogenase, which they could follow by time-resolved serial synchrotron crystallography. Snapshots of the reaction revealed large allosteric motions between the two active sites of the dimeric enzyme. Each active site traded the ability to bind substrate and catalyze the reaction, such that only one was engaged at a time. This behavior is common in enzymes but is rarely visualized and still poorly understood. Science , this issue p. [1167][1] [1]: /lookup/doi/10.1126/science.aaw9904
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