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Issue 34, 2018
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Regulation of both the structure and function by a de novo designed disulfide bond: a case study of heme proteins in myoglobin

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Abstract

A de novo designed intramolecular disulfide bond in myoglobin, resembling that in cytoglobin without structural evidence, was confirmed by an X-ray structure for the first time and was demonstrated to regulate both the structure and function of this protein, which fulfills the design of an artificial dehaloperoxidase, with an activity exceeding that of a native enzyme.

Graphical abstract: Regulation of both the structure and function by a de novo designed disulfide bond: a case study of heme proteins in myoglobin

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Publication details

The article was received on 28 Feb 2018, accepted on 03 Apr 2018 and first published on 04 Apr 2018


Article type: Communication
DOI: 10.1039/C8CC01646A
Citation: Chem. Commun., 2018,54, 4356-4359
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    Regulation of both the structure and function by a de novo designed disulfide bond: a case study of heme proteins in myoglobin

    L. Yin, H. Yuan, K. Du, B. He, S. Gao, G. Wen, X. Tan and Y. Lin, Chem. Commun., 2018, 54, 4356
    DOI: 10.1039/C8CC01646A

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