Expansion of Redox Chemistry in Designer Metalloenzymes

Accounts of Chemical Research
Yang YuJiangyun Wang

Abstract

Many artificial enzymes that catalyze redox reactions have important energy, environmental, and medical applications. Native metalloenzymes use a set of redox-active amino acids and cofactors as redox centers, with a potential range between -700 and +800 mV versus standard hydrogen electrode (SHE, all reduction potentials are versus SHE). The redox potentials and the orientation of redox centers in native metalloproteins are optimal for their redox chemistry. However, the limited number and potential range of native redox centers challenge the design and optimization of novel redox chemistry in metalloenzymes. Artificial metalloenzymes use non-native redox centers and could go far beyond the natural range of redox potentials for novel redox chemistry. In addition to designing protein monomers, strategies for increasing the electron transfer rate in self-assembled protein complexes and protein-electrode or -nanomaterial interfaces will be discussed. Redox reactions in proteins occur on redox active amino acid residues (Tyr, Trp, Met, Cys, etc.) and cofactors (iron sulfur clusters, flavin, heme, etc.). The redox potential of these redox centers cover a ∼1.5 V range and is optimized for their specific functions. Despite recent pro...Continue Reading

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Jul 8, 2020·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Tomoki Himiyama, Yasunori Okamoto
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Sep 12, 2019·Journal of the American Chemical Society·Shuke WuThomas R Ward
Oct 16, 2021·Biological Chemistry·Paul Ebensperger, Claudia Jessen-Trefzer

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