Neuroglobin is capable of self-oxidation of methionine64 introduced at the heme axial position
Author:
Affiliation:
1. School of Chemistry and Chemical Engineering
2. University of South China
3. Hengyang 421001
4. China
5. Liaocheng University
6. Liaocheng 252059
7. Laboratory of Protein Structure and Function
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.
Funder
National Natural Science Foundation of China
Publisher
Royal Society of Chemistry (RSC)
Subject
Inorganic Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2018/DT/C8DT02397B
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