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. Author manuscript; available in PMC: 2022 Aug 1.
Published in final edited form as: Chem Rev. 2022 Jan 25;122(14):12207–12243. doi: 10.1021/acs.chemrev.1c00915

Figure 1.

Figure 1.

Comparison of second-sphere effects in metalloenzymes and metallozeolites. (A) Cu···Cu distance set by protein constraints. (B) Cu···Cu distance set by zeolite lattice. (C) Entatic state of Fe-Met bond in cytochrome c. (D) Entatic state of α-O in iron zeolites. (E) Stabilization of phenolic substrate in Tyr. (F) Stabilization of methane in copper zeolites. (G) Steric barrier in protein pocket (blue) leading to rebound of radical. (H) Steric barrier in zeolite cage (blue) leading to rebound of radical.