Iron(II)- and α-ketoglutarate-dependent (Fe/αKG) enzymes catalyze a large array of reactions. Although hydroxylation reaction catalyzed by these enzymes has been investigated in great details, involving the ferryl (Fe^IV=O) as a key reactive intermediate. The mechanisms of reactions other than hydroxylation are still largely unknown. By using a combined biochemical, bio-organic, and spectroscopic approach, we have studied the mechanisms of two newly discovered Fe/αKG enzymes, FtmOx1 (endoperoxidase) and AsqJ (desaturase/epoxidase), revealing their strategies in controlling reactivity, namely the effect of redox/polar residues near the iron center, the electronic properties of the substrate, and the intrinsic reactivity of the ferryl intermediate.

铁（II）和α-酮戊二酸依赖性（Fe /αKG）酶催化大量反应。尽管已经详细研究了由这些酶催化的羟基化反应，其中涉及到作为主要反应性中间体的小轮（Fe ^IV = O）。除羟基化以外的反应机理仍是未知的。通过结合使用生物化学，生物有机和光谱学方法，我们研究了两种新发现的Fe /αKG酶FtmOx1（内过氧化物酶）和AsqJ（去饱和酶/环氧酶）的机制，揭示了它们控制反应性的策略，即效果铁中心附近的氧化还原/极性残留物，底物的电子性质以及小轮中间体的固有反应性。