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

Abstract

Neuroglobin (Ngb), with 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.

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Publication details

The article was received on 11 Jun 2018, accepted on 13 Jul 2018 and first published on 14 Jul 2018


Article type: Communication
DOI: 10.1039/C8DT02397B
Citation: Dalton Trans., 2018, Accepted Manuscript
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    Neuroglobin is capable of self-oxidation of methionine64 introduced at the heme axial position

    H. Liu, L. Li, B. He, S. Gao, G. Wen and Y. Lin, Dalton Trans., 2018, Accepted Manuscript , DOI: 10.1039/C8DT02397B

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