Evan N. Mirts

A designed heme-[4Fe-4S] metalloenzyme catalyzes sulfite reduction like the native enzyme

Yi Lu, P. Hosseinzadeh, I. Petrik, 2018, Science.

Understanding and Modulating Metalloenzymes with Unnatural Amino Acids, Non-Native Metal Ions, and Non-Native Metallocofactors.

Yi Lu, A. Bhagi-Damodaran, E. Mirts, 2019, Accounts of chemical research.

Molecular understanding of heteronuclear active sites in heme-copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling.

Yi Lu, E. Mirts, C. Reed, 2021, Chemical Society reviews.

Design of Heteronuclear Metalloenzymes.

Yi Lu, Y. Lu, P. Hosseinzadeh, 2016, Methods in enzymology.

Why copper is preferred over iron for oxygen activation and reduction in haem-copper oxidases.

Yi Lu, S. Chakraborty, Yong Zhang, 2017, Nature chemistry.

Heme redox potentials hold the key to reactivity differences between nitric oxide reductase and heme-copper oxidase

Yi Lu, Yong Zhang, P. Hosseinzadeh, 2018, Proceedings of the National Academy of Sciences.

Manganese and Cobalt in the Nonheme-Metal-Binding Site of a Biosynthetic Model of Heme-Copper Oxidase Superfamily Confer Oxidase Activity through Redox-Inactive Mechanism.

Matthew O. Ross, Yi Lu, S. Chakraborty, 2017, Journal of the American Chemical Society.

Enhancing Mn(II)-Binding and Manganese Peroxidase Activity in a Designed Cytochrome c Peroxidase through Fine-Tuning Secondary-Sphere Interactions.

E. Tajkhorshid, Yi Lu, H. Robinson, 2016, Biochemistry.