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

ABSTRACT: 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-SO₂H). 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-SO₂H) were able to be labeled by chemicals, which provided useful platforms to generate artificial proteins.

SUBMITTER: Dai W

PROVIDER: S-EPMC10170655 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature

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

Dai Wei W Yuan Hong H Wang Xiao-Juan XJ Gao Shu-Qin SQ Tan Xiangshi X Lin Ying-Wu YW

RSC chemical biology 20230215 5

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<sub>2</sub>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<sub>2</sub>H) were able to be labeled by chemicals, which provided useful platforms to gen ...[more]

PMID: 37181634

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