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

Authors :
Li-Juan Sun
Hong Yuan
Lu Yu
Shu-Qin Gao
Ge-Bo Wen
Xiangshi Tan
Ying-Wu Lin
Source :
Chemical communications (Cambridge, England). 58(39)
Publication Year :
2022

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.

Details

ISSN :
1364548X
Volume :
58
Issue :
39
Database :
OpenAIRE
Journal :
Chemical communications (Cambridge, England)
Accession number :
edsair.doi.dedup.....7c511032398ba3a71fa0677ca00d5a8d