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Engineering Human Neuroglobin into a Cytochrome c‐Like Protein with a Single Thioether Bond in Non‐native State

Von Wiley-VCH zur Verfügung gestellt

Non-native state: A double mutant of human H64M/V71C neuroglobin (Ngb) was engineered, which formed a single thioether bond as that in atypical cytochrome c (Cyt c), whereas the heme distal Met64 was oxidized to both sulfoxide (SO-Met) and sulfone (SO2-Met), representing a non-native state of Cyt c.


Abstract

A double mutant of human H64M/V71C neuroglobin (Ngb) was engineered, which formed a single thioether bond as that in atypical cytochrome c, whereas the heme distal Met64 was oxidized to both sulfoxide (SO-Met) and sulfone (SO2-Met). By contrast, no Cys-heme cross-link was formed in V71C Ngb with His64/His96 coordination, as shown by the X-ray crystal structure, which indicates that an open distal site facilitates the activation of heme iron for structural modifications.

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