Literature DB >> 30027178

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

Hai-Xiao Liu1, Lianzhi Li, Bo He, Shu-Qin Gao, Ge-Bo Wen, Ying-Wu Lin.   

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.

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Year:  2018        PMID: 30027178     DOI: 10.1039/c8dt02397b

Source DB:  PubMed          Journal:  Dalton Trans        ISSN: 1477-9226            Impact factor:   4.390


  3 in total

1.  Replacement of the heme axial lysine as a test of conformational adaptability in the truncated hemoglobin THB1.

Authors:  Dillon B Nye; Eric A Johnson; Melissa H Mai; Juliette T J Lecomte
Journal:  J Inorg Biochem       Date:  2019-09-04       Impact factor: 4.155

2.  The importance of Asn52 in the structure-function relationship of human cytochrome c.

Authors:  Dan Lou; Xi-Chun Liu; Xiao-Juan Wang; Shu-Qin Gao; Ge-Bo Wen; Ying-Wu Lin
Journal:  RSC Adv       Date:  2020-12-18       Impact factor: 4.036

3.  Enhancement of protein stability by an additional disulfide bond designed in human neuroglobin.

Authors:  Hai-Xiao Liu; Lianzhi Li; Xin-Zhi Yang; Chuan-Wan Wei; Hui-Min Cheng; Shu-Qin Gao; Ge-Bo Wen; Ying-Wu Lin
Journal:  RSC Adv       Date:  2019-01-31       Impact factor: 4.036

  3 in total

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