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Issue 34, 2018

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

Supplementary files

Article information


Submitted
28 Feb 2018
Accepted
03 Apr 2018
First published
04 Apr 2018

Chem. Commun., 2018,54, 4356-4359
Article type
Communication

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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