Michelle L. Kennedy

Metalloprotein and redox protein design

Metalloprotein and redox protein design are rapidly advancing toward the chemical synthesis of novel proteins that have predictable structures and functions. Current data demonstrate a breadth of successful approaches to metallopeptide and metalloprotein design based on de novo, rational and combinatorial strategies. These sophisticated synthetic analogs of natural proteins constructively test our comprehension of metalloprotein structure/function relationships. Additionally, designed redox proteins provide novel constructs for examining the thermodynamics and kinetics of biological electron transfer.

Thermodynamic characterization of ferric and ferrous haem binding to a designed four-α-helix protein

The thermodynamics of ferric and ferrous haem affinity of a de novo designed four-alpha-helix bundle protein and the associated haem electrochemistry is described.

The bis-p-nitrophenyl ester of iron(iii) mesoporphyrin IIacetate: preparation and incorporation into a model hemoprotein

A method for cleanly inserting iron into the bis-p-nitrophenyl ester of mesoporphyrin II, and use of the highly soluble product in the synthesis of a model hemoprotein, is reported.