Iron(II)- and 2-(oxo)-glutarate- (Fe/2OG) dependent oxygenases constitute a large and functionally diverse family of oxidative tailoring enzymes. While most superfamily members are hydroxylases, many other outcomes are possible including halogenation, stereoinversion, cyclization, and desaturation reactions. The structural adaptations that enable alternative transformations are not fully understood. All Fe/2OG enzymes, regardless of outcome, proceed through an Fe(IV)-oxo intermediate that has been evaluated in solution but was previously uncharacterized by x-ray crystallography. We have determined high-resolution x-ray crystal structures of four distinct states in the reaction pathway of an Fe/2OG hydroxylase, including a previously unobserved intermediate complex. The study reveals key second-sphere structural changes that occur at specific stages of the reaction cycle, rationalizing known reactivity patterns in Fe/2OG enzymes.

X-ray crystallographic characterization of the reaction cycle in an iron(II) and 2-(oxo)-glutarate-dependent oxygenase

255th National Meeting (2018)

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