Structural and functional regulations by a disulfide bond designed in myoglobin like human neuroglobin

Abstract

An artificial disulfide bond (Cys46–Cys61) was designed in the heme distal site of myoglobin, which regulates the conformation of the heme distal His64 and the protein reactivity, as confirmed by X-ray crystallography, EPR, and kinetic UV-vis studies. This study shows the successful design of a disulfide bond with suitable positions in globins, conferring a structure and function like those of the native human neuroglobin.