Self-oxidation of cysteine to sulfinic acid in an engineered T67C myoglobin: structure and reactivity

Myoglobin (Mb) was found to undergo self-oxidation when a cysteine residue was engineered at position 67 in the heme distal site. Both the X-ray crystal structure and mass spectrum confirmed the formation of a sulfinic acid (Cys–SO(2)H). Moreover, the self-oxidation could be controlled during protei...

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Detalles Bibliográficos
Autores principales: Dai, Wei, Yuan, Hong, Wang, Xiao-Juan, Gao, Shu-Qin, Tan, Xiangshi, Lin, Ying-Wu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: RSC 2023
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10170655/
https://www.ncbi.nlm.nih.gov/pubmed/37181634
http://dx.doi.org/10.1039/d3cb00007a
Descripción
Sumario:Myoglobin (Mb) was found to undergo self-oxidation when a cysteine residue was engineered at position 67 in the heme distal site. Both the X-ray crystal structure and mass spectrum confirmed the formation of a sulfinic acid (Cys–SO(2)H). Moreover, the self-oxidation could be controlled during protein purification to yield the unmodified form (T67C Mb). Importantly, both T67C Mb and T67C Mb (Cys–SO(2)H) were able to be labeled by chemicals, which provided useful platforms to generate artificial proteins.

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