Neuroglobin is capable of self-oxidation of methionine64 introduced at the heme axial position. Issue 32 (20th July 2018)

• Record Type: Journal Article
• Authors: Liu, Hai-Xiao; Li, Lianzhi; He, Bo; Gao, Shu-Qin; Wen, Ge-Bo; Lin, Ying-Wu
• Is Part Of: Dalton transactions. Volume 47:Issue 32(2018)
• Page Start: 10847
• Page End: 10852
• Publication Date: 2018-07-20
• Subjects: Chemistry, Inorganic -- Periodicals; Chemistry, Physical and theoretical -- Periodicals; Chemistry, Inorganic -- Periodicals; 546.05
• DOI: 10.1039/c8dt02397b
• Languages: English
• ISSNs: 1477-9226

Abstract

Abstract : The H64M neuroglobin mutant adopts a high-spin heme state and is capable of self-oxidation of the heme axial Met64, producing both methionine sulfoxide (SO-Met) and sulfone (SO2 -Met), which represents the structure and function of cytochrome c in a non-native state. Abstract : Neuroglobin (Ngb), with its physiological role not fully understood, was found to be capable of self-oxidation of methionine64 introduced at the heme axial position (H64M Ngb), adopting a high-spin heme state and producing both methionine sulfoxide (SO-Met) and sulfone (SO2 -Met), which represents the structure and function of cytochrome c in a non-native state.