Neuroglobin is capable of self-oxidation of methionine64 introduced at the heme axial position

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 (SO 2 -Met), which represents...

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Veröffentlicht in:	Dalton transactions : an international journal of inorganic chemistry 2018-08, Vol.47 (32), p.1847-1852
Hauptverfasser:	Liu, Hai-Xiao, Li, Lianzhi, He, Bo, Gao, Shu-Qin, Wen, Ge-Bo, Lin, Ying-Wu
Format:	Artikel
Sprache:	eng
Schlagworte:	Coordination Complexes - chemistry Coordination Complexes - metabolism Cytochromes Escherichia coli - genetics Heme - chemistry Heme - metabolism Humans Iron - metabolism Ligands Methionine Methionine - analogs & derivatives Methionine - metabolism Molecular Conformation Mutation Neuroglobin - chemistry Neuroglobin - genetics Neuroglobin - metabolism Oxidation Oxidation-Reduction Oxygen - metabolism Protein Binding Sulfones - metabolism
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Zusammenfassung:	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 (SO 2 -Met), which represents the structure and function of cytochrome c in a non-native state. 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 (SO 2 -Met), which represents the structure and function of cytochrome c in a non-native state.
ISSN:	1477-9226 1477-9234
DOI:	10.1039/c8dt02397b