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Unique Tyr-heme double cross-links in F43Y/T67R myoglobin: an artificial enzyme with a peroxidase activity comparable to that of native peroxidases

Abstract

An X-ray crystal structure of F43Y/T67R myoglobin revealed unique Tyr-heme double cross-links between Tyr43 and the heme 4-vinyl group, which represents a novel post-translational modification of heme proteins. Moreover, with a feature of distal His-Arg pair, the designed artificial enzyme exhibited a peroxidase activity comparable to that of native peroxidases, such as the most efficient horseradish peroxidase.

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Supplementary files

Publication details

The article was received on 08 Apr 2019, accepted on 15 May 2019 and first published on 15 May 2019


Article type: Communication
DOI: 10.1039/C9CC02714A
Chem. Commun., 2019, Accepted Manuscript

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    Unique Tyr-heme double cross-links in F43Y/T67R myoglobin: an artificial enzyme with a peroxidase activity comparable to that of native peroxidases

    C. Liu, H. Yuan, F. Liao, C. Wei, K. Du, S. Gao, X. Tan and Y. Lin, Chem. Commun., 2019, Accepted Manuscript , DOI: 10.1039/C9CC02714A

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